Molecular chirality mediated amyloid formation on phospholipid surfaces

Xue Wang, Cunli Wang, Huiying Chu, Haijuan Qin, Dongdong Wang, Feifei Xu, Xuanjun Ai, Chunshan Quan, Guohui Li and Guangyan Qing

Chem. Sci., 2020, 11, 7369
DOI: 10.1039/D0SC02212H

Aggregation, structure and water permeability of membrane-embedded helical Aβ oligomers

Ke Wang and Wensheng Cai

Phys. Chem. Chem. Phys., 2024, 26, 5128
DOI: 10.1039/D3CP05317B

Role of the carboxy groups of triterpenoids in their inhibition of the nucleation of amyloid β42 required for forming toxic oligomers

Kazuma Murakami, Takuya Yoshioka, Shiori Horii, Mizuho Hanaki, Satohiro Midorikawa, Shinji Taniwaki, Hiroki Gunji, Ken-ichi Akagi, Taiji Kawase, Kenji Hirose and Kazuhiro Irie

Chem. Commun., 2018, 54, 6272
DOI: 10.1039/C8CC03230K

Impact of sphingosine and acetylsphingosines on the aggregation and toxicity of metal-free and metal-treated amyloid-β

Yelim Yi, Yuxi Lin, Jiyeon Han, Hyuck Jin Lee, Nahye Park, Geewoo Nam, Young S. Park, Young-Ho Lee and Mi Hee Lim

Chem. Sci., 2021, 12, 2456
DOI: 10.1039/D0SC04366D

Dynamic micellar oligomers of amyloid beta peptides play a crucial role in their aggregation mechanisms

Bertrand Morel, Maria Paz Carrasco, Samuel Jurado, Carmen Marco and Francisco Conejero-Lara

Phys. Chem. Chem. Phys., 2018, 20, 20597
DOI: 10.1039/C8CP02685H

Improved δ-valerolactam templates for the assembly of Aβ-miniamyloids by boronic ester formation

André Wuttke, Sebastian Nils Fischer, Annika Nebel, Michael Marsch and Armin Geyer

Org. Biomol. Chem., 2016, 14, 5032
DOI: 10.1039/C6OB00565A

A time-resolved study on the interaction of oppositely charged bicelles – implications on the charged lipid exchange kinetics

Po-Wei Yang, Tsang-Lang Lin, Yuan Hu and U-Ser Jeng

Soft Matter, 2015, 11, 2237
DOI: 10.1039/C4SM02886D

Nanomaterial synthesis, an enabler of amyloidosis inhibition against human diseases

Nicholas Andrikopoulos, Yuhuan Li, Luca Cecchetto, Aparna Nandakumar, Tatiana Da Ros, Thomas P. Davis, Kelly Velonia and Pu Chun Ke

Nanoscale, 2020, 12, 14422
DOI: 10.1039/D0NR04273K

Metal complexes for multimodal imaging of misfolded protein-related diseases

S. Lacerda, J.-F. Morfin, C. F. G. C. Geraldes and É. Tóth

Dalton Trans., 2017, 46, 14461
DOI: 10.1039/C7DT02371E

Chiral supramolecular coordination cages as high-performance inhibitors against amyloid-β aggregation

Ling-Yu Bao, Si-Jia Hao, Sai-Fei Xi, Xiaodong Yan, Hai-Xia Zhang, Rui Shen and Zhi-Guo Gu

Chem. Commun., 2018, 54, 8725
DOI: 10.1039/C8CC04913K

Nanoscopic insights into the surface conformation of neurotoxic amyloid β oligomers

Martina Banchelli, Roberta Cascella, Cristiano D'Andrea, Leszek Cabaj, Iacopo Osticioli, Daniele Ciofini, Mai Suan Li, Krzysztof Skupień, Marella de Angelis, Salvatore Siano, Cristina Cecchi, Roberto Pini, Giovanni La Penna, Fabrizio Chiti and Paolo Matteini

RSC Adv., 2020, 10, 21907
DOI: 10.1039/D0RA03799K

Chemical strategies to modify amyloidogenic peptides using iridium(iii) complexes: coordination and photo-induced oxidation

Juhye Kang, Jung Seung Nam, Hyuck Jin Lee, Geewoo Nam, Hyun-Woo Rhee, Tae-Hyuk Kwon and Mi Hee Lim

Chem. Sci., 2019, 10, 6855
DOI: 10.1039/C9SC00931K

A cationic amphiphilic peptide chaperone rescues Aβ42 aggregation and cytotoxicity

DRGKoppalu R. Puneeth Kumar, Rahi M. Reja, Dillip K. Senapati, Manjeet Singh, Sachin A. Nalawade, Gijo George, Grace Kaul, Abdul Akhir, Sidharth Chopra, Srinivasarao Raghothama and Hosahudya N. Gopi

RSC Med. Chem., 2023, 14, 332
DOI: 10.1039/D2MD00414C

Molecular understanding of a potential functional link between antimicrobial and amyloid peptides

Mingzhen Zhang, Jun Zhao and Jie Zheng

Soft Matter, 2014, 10, 7425
DOI: 10.1039/C4SM00907J

A cationic polymethacrylate-copolymer acts as an agonist for β-amyloid and an antagonist for amylin fibrillation

Bikash R. Sahoo, Takuya Genjo, Takahiro W. Nakayama, Andrea K. Stoddard, Toshio Ando, Kazuma Yasuhara, Carol A. Fierke and Ayyalusamy Ramamoorthy

Chem. Sci., 2019, 10, 3976
DOI: 10.1039/C8SC05771K

Pathogenic properties of Alzheimer's β-amyloid identified from structure–property patient-phenotype correlations

Manish K. Tiwari and Kasper P. Kepp

Dalton Trans., 2015, 44, 2747
DOI: 10.1039/C4DT03122A

Ultraviolet irradiation-mediated formation of Aβ42oligomers and reactive oxygen species in Zn2+-bound Aβ42aggregates irrespective of the removal of Zn2+

Xiang Li, Xiongwei Dong, Yaojing Liu, Yan Meng, Yong Zhang, Dan Zhang and Changlin Liu

New J. Chem., 2016, 40, 9385
DOI: 10.1039/C6NJ02004F

Polymorphic cross-seeding amyloid assemblies of amyloid-β and human islet amyloid polypeptide

Mingzhen Zhang, Rundong Hu, Hong Chen, Yung Chang, Jie Ma, Guizhao Liang, Jingyan Mi, Yaru Wang and Jie Zheng

Phys. Chem. Chem. Phys., 2015, 17, 23245
DOI: 10.1039/C5CP03329B

Applications of liquid crystals in biosensing

Ziyihui Wang, Tianhua Xu, Adam Noel, Yu-Cheng Chen and Tiegen Liu

Soft Matter, 2021, 17, 4675
DOI: 10.1039/D0SM02088E

Binding of protofibrillar Aβ trimers to lipid bilayer surface enhances Aβ structural stability and causes membrane thinning

Xuewei Dong, Yunxiang Sun, Guanghong Wei, Ruth Nussinov and Buyong Ma

Phys. Chem. Chem. Phys., 2017, 19, 27556
DOI: 10.1039/C7CP05959K

How do salt and lipids affect conformational dynamics of Aβ42 monomers in water?

Brian Andrews, Thomas Ruggiero and Brigita Urbanc

Phys. Chem. Chem. Phys., 2023, 25, 2566
DOI: 10.1039/D2CP05044G

All-atom molecular dynamics simulations of the combined effects of different phospholipids and cholesterol content on electroporation

Fei Guo, Ji Wang, Jiong Zhou, Kun Qian, Hongchun Qu, Ping Liu and Shidong Zhai

RSC Adv., 2022, 12, 24491
DOI: 10.1039/D2RA03895A

A β-barrel-like tetramer formed by a β-hairpin derived from Aβ

Tuan D. Samdin, Chelsea R. Jones, Gretchen Guaglianone, Adam G. Kreutzer, J. Alfredo Freites, Michał Wierzbicki and James S. Nowick

Chem. Sci., 2024, 15, 285
DOI: 10.1039/D3SC05185D

In silico phase separation in the presence of GM1 in ternary and quaternary lipid bilayers

Ipsita Basu and Chaitali Mukhopadhyay

Phys. Chem. Chem. Phys., 2015, 17, 17130
DOI: 10.1039/C5CP01970B

The size-effect of gold nanoparticles and nanoclusters in the inhibition of amyloid-β fibrillation

Guanbin Gao, Mingxi Zhang, Dejun Gong, Rui Chen, Xuejiao Hu and Taolei Sun

Nanoscale, 2017, 9, 4107
DOI: 10.1039/C7NR00699C

Graphene quantum dots obstruct the membrane axis of Alzheimer's amyloid beta

Huayuan Tang, Yuhuan Li, Aleksandr Kakinen, Nicholas Andrikopoulos, Yunxiang Sun, Eunbi Kwak, Thomas P. Davis, Feng Ding and Pu Chun Ke

Phys. Chem. Chem. Phys., 2022, 24, 86
DOI: 10.1039/D1CP04246G

Nanoscale insights into the local structural rearrangements of amyloid-β induced by bexarotene

Kamila Sofińska, Piotr Batys, Adrian Cernescu, Dhiman Ghosh, Katarzyna Skirlińska-Nosek, Jakub Barbasz, Sara Seweryn, Natalia Wilkosz, Roland Riek, Marek Szymoński and Ewelina Lipiec

Nanoscale, 2023, 15, 14606
DOI: 10.1039/D3NR01608K

Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory

Hyun Joon Chang, Myeongsang Lee, Jae In Kim, Gwonchan Yoon and Sungsoo Na

Phys. Chem. Chem. Phys., 2017, 19, 11492
DOI: 10.1039/C7CP01418J

Biophysical insights into the membrane interaction of the core amyloid-forming Aβ40fragment K16–K28 and its role in the pathogenesis of Alzheimer's disease

Swapna Bera, Kyle J. Korshavn, Rajiv K. Kar, Mi Hee Lim, Ayyalusamy Ramamoorthy and Anirban Bhunia

Phys. Chem. Chem. Phys., 2016, 18, 16890
DOI: 10.1039/C6CP02023B

Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation

Kyle J. Korshavn, Anirban Bhunia, Mi Hee Lim and Ayyalusamy Ramamoorthy

Chem. Commun., 2016, 52, 882
DOI: 10.1039/C5CC08634E

Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers

Bruno C. Borro, Lucia Parolini, Pietro Cicuta, Vito Foderà and Lorenzo Di Michele

Phys. Chem. Chem. Phys., 2017, 19, 27930
DOI: 10.1039/C7CP05339H

Synthesis and biochemical characterization of quasi-stable trimer models of full-length amyloid β40 with a toxic conformation

Yumi Irie, Mizuho Hanaki, Kazuma Murakami, Tsuneo Imamoto, Takumi Furuta, Takeo Kawabata, Taiji Kawase, Kenji Hirose, Yoko Monobe, Ken-ichi Akagi, Ryo C. Yanagita and Kazuhiro Irie

Chem. Commun., 2019, 55, 182
DOI: 10.1039/C8CC08618D

Peptide-functionalized nanocapsules for targeted inhibition of β2-microglobulin amyloid aggregation

Lin Tang, Miao Sun, Junnan Chen, Qiong Dai, Song Xue, Chaoyong Liu and Ming Zhang

J. Mater. Chem. B, 2025, 13, 3319
DOI: 10.1039/D4TB01347F

Atomic resolution map of the soluble amyloid beta assembly toxic surfaces

Rashik Ahmed, Michael Akcan, Adree Khondker, Maikel C. Rheinstädter, José C. Bozelli, Richard M. Epand, Vincent Huynh, Ryan G. Wylie, Stephen Boulton, Jinfeng Huang, Chris P. Verschoor and Giuseppe Melacini

Chem. Sci., 2019, 10, 6072
DOI: 10.1039/C9SC01331H

Cascade autohydrolysis of Alzheimer's Aβ peptides

Martin Wolfram, Manish K. Tiwari, Tue Hassenkam, Ming Li, Morten J. Bjerrum and Morten Meldal

Chem. Sci., 2023, 14, 4986
DOI: 10.1039/D2SC06668H

Understanding structural characteristics of out-of-register hIAPP amyloid proteins via molecular dynamics

Inchul Baek, Myeongsang Lee and Sungsoo Na

RSC Adv., 2016, 6, 77666
DOI: 10.1039/C6RA19100B

Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways

F. Bellia, V. Lanza, S. García-Viñuales, I. M. M. Ahmed, A. Pietropaolo, C. Iacobucci, G. Malgieri, G. D'Abrosca, R. Fattorusso, V. G. Nicoletti, D. Sbardella, G. R. Tundo, M. Coletta, L. Pirone, E. Pedone, D. Calcagno, G. Grasso and D. Milardi

Chem. Sci., 2019, 10, 2732
DOI: 10.1039/C8SC03394C

Model membrane size-dependent amyloidogenesis of Alzheimer's amyloid-β peptides

Misaki Kinoshita, Erina Kakimoto, Mayu S. Terakawa, Yuxi Lin, Tatsuya Ikenoue, Masatomo So, Toshihiko Sugiki, Ayyalusamy Ramamoorthy, Yuji Goto and Young-Ho Lee

Phys. Chem. Chem. Phys., 2017, 19, 16257
DOI: 10.1039/C6CP07774A

Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers

Mingzhen Zhang, Rundong Hu, Hong Chen, Yung Chang, Xiong Gong, Fufeng Liu and Jie Zheng

Phys. Chem. Chem. Phys., 2015, 17, 10373
DOI: 10.1039/C4CP05658B

Recent developments in the chemical biology of amyloid-β oligomer targeting

Yalin Wang, Jiefang Chen, Furong Gao, Ming Hu and Xiaohui Wang

Org. Biomol. Chem., 2023, 21, 4540
DOI: 10.1039/D3OB00509G

The mechanical response of hIAPP nanowires based on different bending direction simulations

J. I. Kim, M. Lee, I. Baek, G. Yoon and S. Na

Phys. Chem. Chem. Phys., 2014, 16, 18493
DOI: 10.1039/C4CP02494J

Charge effects at nano-bio interfaces: a model of charged gold nanoclusters on amylin fibrillation

Xintong Tang, Guanbin Gao, Ting Zhang, Jianhang Li, Meng Yu, Meng He and Taolei Sun

Nanoscale, 2020, 12, 18834
DOI: 10.1039/D0NR03877F

Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism

Torsten John, Stefania Piantavigna, Tiara J. A. Dealey, Bernd Abel, Herre Jelger Risselada and Lisandra L. Martin

Chem. Sci., 2023, 14, 3730
DOI: 10.1039/D3SC00159H

Conformation-specific perturbation of membrane dynamics by structurally distinct oligomers of Alzheimer's amyloid-β peptide

Priyanka Madhu, Debapriya Das and Samrat Mukhopadhyay

Phys. Chem. Chem. Phys., 2021, 23, 9686
DOI: 10.1039/D0CP06456D

Monitoring the formation of a colloidal lipid gel at the nanoscale: vesicle aggregation driven by a temperature-induced mechanism

Kirian Talló, Ramon Pons, César González and Olga López

J. Mater. Chem. B, 2021, 9, 7472
DOI: 10.1039/D1TB01020D

Aβ aggregation behavior at interfaces with switchable wettability: a bioinspired perspective to understand amyloid formation

Yijia Guan, Dongqin Yu, Hanjun Sun, Jinsong Ren and Xiaogang Qu

Chem. Commun., 2021, 57, 2641
DOI: 10.1039/D0CC07546A

Alzheimer's amyloid-beta intermediates generated using polymer-nanodiscs

Bikash R. Sahoo, Takuya Genjo, Michael Bekier, Sarah J. Cox, Andrea K. Stoddard, Magdalena Ivanova, Kazuma Yasuhara, Carol A. Fierke, Yanzhuang Wang and Ayyalusamy Ramamoorthy

Chem. Commun., 2018, 54, 12883
DOI: 10.1039/C8CC07921H

Membrane analysis with amphiphilic carbon dots

Sukhendu Nandi, Ravit Malishev, Kaviya Parambath Kootery, Yelena Mirsky, Sofiya Kolusheva and Raz Jelinek

Chem. Commun., 2014, 50, 10299
DOI: 10.1039/C4CC03504F

On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides

Marianna Flora Tomasello, Alessandro Sinopoli and Giuseppe Pappalardo

Journal of Diabetes Research, 2015, 2015, 1
DOI: 10.1155/2015/918573

The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage

Cecilia Wallin, Yoshitaka Hiruma, Sebastian K. T. S. Wärmländer, Isabelle Huvent, Jüri Jarvet, Jan Pieter Abrahams, Astrid Gräslund, Guy Lippens and Jinghui Luo

J. Am. Chem. Soc., 2018, 140, 8138
DOI: 10.1021/jacs.7b13623

Monitoring the Conformational Changes of the Aβ(25−35) Peptide in SDS Micelles: A Matter of Time

Angelo Santoro, Michela Buonocore, Manuela Grimaldi, Enza Napolitano and Anna Maria D’Ursi

IJMS, 2023, 24, 971
DOI: 10.3390/ijms24020971

High-Throughput Screening at the Membrane Interface Reveals Inhibitors of Amyloid-β

Sarah J. Cox, Brian Lam, Ajay Prasad, Hannah A. Marietta, Nicholas V. Stander, Joseph G. Joel, Bikash R. Sahoo, Fucheng Guo, Andrea K. Stoddard, Magdalena I. Ivanova and Ayyalusamy Ramamoorthy

Biochemistry, 2020, 59, 2249
DOI: 10.1021/acs.biochem.0c00328

Interaction of the tau fibrils with the neuronal membrane

Unmesh D. Chowdhury, Arnav Paul and B.L. Bhargava

Biophysical Chemistry, 2023, 298, 107024
DOI: 10.1016/j.bpc.2023.107024

Using mass spectrometry‐based methods to understand amyloid formation and inhibition of alpha‐synuclein and amyloid beta

Wesley J. Wagner and Michael L. Gross

Mass Spectrometry Reviews, 2024, 43, 782
DOI: 10.1002/mas.21814

Amyloidβ Peptides in interaction with raft-mime model membranes: a neutron reflectivity insight

Valeria Rondelli, Paola Brocca, Simona Motta, Massimo Messa, Laura Colombo, Mario Salmona, Giovanna Fragneto, Laura Cantù and Elena Del Favero

Sci Rep, 2016, 6
DOI: 10.1038/srep20997

Interactions of polyunsaturated fatty acids with amyloid peptides Aβ40 and Aβ42

Amna El Shatshat, Amy Trinh Pham and Praveen P.N. Rao

Archives of Biochemistry and Biophysics, 2019, 663, 34
DOI: 10.1016/j.abb.2018.12.027

The co-effect of copper and lipid vesicles on Aβ aggregation

Xuehang Zhu, Wenjing Liu, Weijing Zhao, Ziwei Chang and Jun Yang

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2023, 1865, 184082
DOI: 10.1016/j.bbamem.2022.184082

Effect of osmolytes on the conformational stability of Aβ(25–35): A circular dichroism analysis

Angelo Santoro, Michela Buonocore and Anna Maria D'Ursi

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2025, 1867, 184420
DOI: 10.1016/j.bbamem.2025.184420

Accelerated Amyloid Aggregation Dynamics of Intrinsically Disordered Proteins in Heavy Water

Myung Kook Son, Dongjoon Im, Da Gyeong Hyun, Soohyeong Kim, So Yeon Chun, Jeong-Mo Choi, Tae Su Choi, Minhaeng Cho, Kyungwon Kwak and Hugh I. Kim

J. Phys. Chem. Lett., 2024, 15, 11823
DOI: 10.1021/acs.jpclett.4c02764

Effect of Lycoris chejuensis and Its Active Components on Experimental Models of Alzheimer’s Disease

Joonki Kim, Yurim Park, Yoon Sun Chun, Jin Wook Cha, Hak Cheol Kwon, Myung Sook Oh, Sungkwon Chung and Hyun Ok Yang

J. Agric. Food Chem., 2015, 63, 6979
DOI: 10.1021/acs.jafc.5b00889

Small molecule NPT-440-1 inhibits ionic flux through Aβ 1-42 pores: Implications for Alzheimer's disease therapeutics

Alan L. Gillman, Joon Lee, Srinivasan Ramachandran, Ricardo Capone, Tania Gonzalez, Wolf Wrasidlo, Eliezer Masliah and Ratnesh Lal

Nanomedicine: Nanotechnology, Biology and Medicine, 2016, 12, 2331
DOI: 10.1016/j.nano.2016.06.001

Structural Characterization of the Amyloid Precursor Protein Transmembrane Domain and Its γ-Cleavage Site

Anna Itkin, Evgeniy S. Salnikov, Christopher Aisenbrey, Jesus Raya, Elise Glattard, Vincent Raussens, Jean-Marie Ruysschaert and Burkhard Bechinger

ACS Omega, 2017, 2, 6525
DOI: 10.1021/acsomega.7b00619

Aggregation and partitioning of amyloid peptide fragments in the presence of a lipid bilayer: A coarse grained molecular dynamics study

Aleksandra Drajkowska and Andrzej Molski

Biophysical Chemistry, 2023, 300, 107051
DOI: 10.1016/j.bpc.2023.107051

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43

Liangzhong Lim, Yuanyuan Wei, Yimei Lu, Jianxing Song and Gregory A. Petsko

PLoS Biol, 2016, 14, e1002338
DOI: 10.1371/journal.pbio.1002338

Copper Toxicity Links to Pathogenesis of Alzheimer’s Disease and Therapeutics Approaches

Hafza Wajeeha Ejaz, Wei Wang and Minglin Lang

IJMS, 2020, 21, 7660
DOI: 10.3390/ijms21207660

Protein Language Pragmatic Analysis and Progressive Transfer Learning for Profiling Peptide-Protein Interactions

Shutao Chen, Ke Yan, Xuelong Li and Bin Liu

IEEE Trans. Neural Netw. Learning Syst., 2025, 36, 15385
DOI: 10.1109/TNNLS.2025.3540291

Effects of End-Terminal Capping on Transthyretin (105–115) Amyloid Protofibrils Using Steered Molecular Dynamics

Myeongsang Lee, Hyunsung Choi and Sungsoo Na

Journal of Nanomaterials, 2016, 2016, 1
DOI: 10.1155/2016/1863065

The amyloid cascade hypothesis: an updated critical review

Kasper P Kepp, Nikolaos K Robakis, Poul F Høilund-Carlsen, Stefano L Sensi and Bryce Vissel

Brain, 2023, 146, 3969
DOI: 10.1093/brain/awad159

Interaction between Multimeric Sulfated Saccharides and Alzheimer Amyloid β (1-42)

Tomohiro Fukuda, Erino Matsumoto and Yoshiko Miura

Chemistry Letters, 2015, 44, 1482
DOI: 10.1246/cl.150633

Interactions between amyloid β peptide and lipid membranes

Zheng Niu, Zhengfeng Zhang, Weijing Zhao and Jun Yang

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1663
DOI: 10.1016/j.bbamem.2018.04.004

Modulation of Alzheimer's amyloid β peptide oligomerization and toxicity by extracellular Hsp70

Isabel Rivera, Ricardo Capone, David M. Cauvi, Nelson Arispe and Antonio De Maio

Cell Stress and Chaperones, 2018, 23, 269
DOI: 10.1007/s12192-017-0839-0

Capping effects on polymorphic Aβ 16–21 amyloids depend on their size: A molecular dynamics simulation study

Myeongsang Lee, Hyun Joon Chang, Hyunsung Choi and Sungsoo Na

Biophysical Chemistry, 2018, 232, 1
DOI: 10.1016/j.bpc.2017.09.003

Acetylation of Aβ42 at Lysine 16 Disrupts Amyloid Formation

Rashmi Adhikari, Mu Yang, Nabanita Saikia, Colina Dutta, Wafa F.A. Alharbi, Zhiying Shan, Ravindra Pandey and Ashutosh Tiwari

ACS Chem. Neurosci., 2020, 11, 1178
DOI: 10.1021/acschemneuro.0c00069

Natural Tripeptide-Based Inhibitor of Multifaceted Amyloid β Toxicity

K. Rajasekhar, Chilakapati Madhu and T. Govindaraju

ACS Chem. Neurosci., 2016, 7, 1300
DOI: 10.1021/acschemneuro.6b00175

Vav2 is a novel APP-interacting protein that regulates APP protein level

Youjia Zhang, Xiaxin Yang, Yongrui Liu, Liang Ge, Jiarong Wang, Xiulian Sun, Bo Wu and Junfeng Wang

Sci Rep, 2022, 12
DOI: 10.1038/s41598-022-16883-z

In vitro coordination of Fe-protoheme with amyloid β is non-specific and exhibits multiple equilibria

Jérôme Gout, Floriane Meuris, Alain Desbois and Pierre Dorlet

Journal of Inorganic Biochemistry, 2022, 227, 111664
DOI: 10.1016/j.jinorgbio.2021.111664

Lysine‐Derived Carbon Dots for Chiral Inhibition of Prion Peptide Fibril Assembly

Elad Arad, Susanta Kumar Bhunia, Jürgen Jopp, Sofiya Kolusheva, Hanna Rapaport and Raz Jelinek

Advanced Therapeutics, 2018, 1
DOI: 10.1002/adtp.201800006

Modulation of Alzheimer’s Aβ Protofilament-Membrane Interactions by Lipid Headgroups

Florentina Tofoleanu, Bernard R. Brooks and Nicolae-Viorel Buchete

ACS Chem. Neurosci., 2015, 6, 446
DOI: 10.1021/cn500277f

Alpha-beta transition induced by C18-conjugation of polyalanine and its implication in aqueous solution behavior of poly(ethylene glycol)-polyalanine block copolymers

Min Hee Park, Jinkyung Park, Hyun Jung Lee and Byeongmoon Jeong

Biomater Res, 2020, 24
DOI: 10.1186/s40824-020-00200-8

Fibrillation mechanism of glucagon in the presence of phospholipid bilayers as revealed by 13C solid-state NMR spectroscopy

Izumi Yamane, Ayano Momose, Hideki Fujita, Eri Yoshimoto, Akie Kikuchi-Kinoshita, Izuru Kawamura and Akira Naito

Chemistry and Physics of Lipids, 2019, 219, 36
DOI: 10.1016/j.chemphyslip.2019.01.008

Comparison of Synthetic Neuronal Model Membrane Mimics in Amyloid Aggregation at Atomic Resolution

Swapna Bera, Nilanjan Gayen, Sk. Abdul Mohid, Dipita Bhattacharyya, Janarthanan Krishnamoorthy, Dibakar Sarkar, Jihye Choi, Nirakar Sahoo, Atin K. Mandal, DongKuk Lee and Anirban Bhunia

ACS Chem. Neurosci., 2020, 11, 1965
DOI: 10.1021/acschemneuro.0c00166

Multivalent display of chemical signals on self‐assembled peptide scaffolds

Hannah E. Distaffen, Christopher W. Jones, Brittany L. Abraham and Bradley L. Nilsson

Peptide Science, 2021, 113
DOI: 10.1002/pep2.24224

Effect of lipid saturation on the topology and oligomeric state of helical membrane polypeptides

Evgeniy Salnikov and Burkhard Bechinger

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2022, 1864, 184001
DOI: 10.1016/j.bbamem.2022.184001

Molecular Recipe for γ-Secretase Modulation from Computational Analysis of 60 Active Compounds

Ning Tang, Arun K. Somavarapu and Kasper P. Kepp

ACS Omega, 2018, 3, 18078
DOI: 10.1021/acsomega.8b02196

Molecular insights into the primary nucleation of polymorphic amyloid β dimers in DOPC lipid bilayer membrane

Olga Press‐Sandler and Yifat Miller

Protein Science, 2022, 31
DOI: 10.1002/pro.4283

Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson’s disease

Istvan Horvath and Pernilla Wittung-Stafshede

Proc. Natl. Acad. Sci. U.S.A., 2016, 113, 12473
DOI: 10.1073/pnas.1610371113

Strategic Design of 2,2′-Bipyridine Derivatives to Modulate Metal–Amyloid-β Aggregation

Yonghwan Ji, Hyuck Jin Lee, Minjeong Kim, Geewoo Nam, Shin Jung C. Lee, Jaeheung Cho, Cheol-Min Park and Mi Hee Lim

Inorg. Chem., 2017, 56, 6695
DOI: 10.1021/acs.inorgchem.7b00782

Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity

Rihards Aleksis, Filips Oleskovs, Kristaps Jaudzems, Jens Pahnke and Henrik Biverstål

Biochimie, 2017, 140, 176
DOI: 10.1016/j.biochi.2017.07.011

Amyloid-β Peptide Triggers Membrane Remodeling in Supported Lipid Bilayers Depending on Their Hydrophobic Thickness

Sigalit Meker, Hokyun Chin, Tun Naw Sut and Nam-Joon Cho

Langmuir, 2018, 34, 9548
DOI: 10.1021/acs.langmuir.8b01196

Direct Delivery of ANA-TA9, a Peptide Capable of Aβ Hydrolysis, to the Brain by Intranasal Administration

Yusuke Hatakawa, Akiko Tanaka, Tomoyuki Furubayashi, Rina Nakamura, Motomi Konishi, Toshifumi Akizawa and Toshiyasu Sakane

Pharmaceutics, 2021, 13, 1673
DOI: 10.3390/pharmaceutics13101673

Membrane-mimetic systems for biophysical studies of the amyloid-β peptide

Nicklas Österlund, Jinghui Luo, Sebastian K.T.S. Wärmländer and Astrid Gräslund

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2019, 1867, 492
DOI: 10.1016/j.bbapap.2018.11.005

Inhibitory effects of magnolol and honokiol on human calcitonin aggregation

Caiao Guo, Liang Ma, Yudan Zhao, Anlin Peng, Biao Cheng, Qiaoqiao Zhou, Ling Zheng and Kun Huang

Sci Rep, 2015, 5
DOI: 10.1038/srep13556

Concentration-Dependent Effects of Cholesterol on the Dimerization of Amyloid-β Peptides in Lipid Bilayers

Bin Wang and Cong Guo

ACS Chem. Neurosci., 2022, 13, 2709
DOI: 10.1021/acschemneuro.2c00349

Amyloid‐β in Alzheimer's disease: Structure, toxicity, distribution, treatment, and prospects

Yifan Yu, Shilong Yu, Giuseppe Battaglia and Xiaohe Tian

Ibrain, 2024
DOI: 10.1002/ibra.12155

Spike Protein Fragments Promote Alzheimer’s Amyloidogenesis

Sujian Cao, Zhiyuan Song, Jinyu Rong, Nicholas Andrikopoulos, Xiufang Liang, Yue Wang, Guotao Peng, Feng Ding and Pu Chun Ke

ACS Appl. Mater. Interfaces, 2023, 15, 40317
DOI: 10.1021/acsami.3c09815

Molecular Insights into the Dynamics of Amyloid Fibril Growth: Elongation and Lateral Assembly of GNNQQNY Protofibrils

Torsten John, Aldo Rampioni, David Poger and Alan E. Mark

ACS Chem. Neurosci., 2024, 15, 716
DOI: 10.1021/acschemneuro.3c00754

In Search of Aggregation Pathways of IAPP and Other Amyloidogenic Proteins: Finding Answers through NMR Spectroscopy

Hiren R. Patel, Amit S. Pithadia, Jeffrey R. Brender, Carol A. Fierke and Ayyalusamy Ramamoorthy

J. Phys. Chem. Lett., 2014, 5, 1864
DOI: 10.1021/jz5001775

Chirality‐Assisted Ring‐Like Aggregation of Aβ(1–40) at Liquid–Solid Interfaces: A Stereoselective Two‐Step Assembly Process

Guanbin Gao, Mingxi Zhang, Pei Lu, Guanlun Guo, Dong Wang and Taolei Sun

Angewandte Chemie, 2015, 127, 2273
DOI: 10.1002/ange.201410768

Study of a Bifunctional Aβ Aggregation Inhibitor with the Abilities of Antiamyloid-β and Copper Chelation

Qian Zhang, Xiaoyu Hu, Wei Wang and Zhi Yuan

Biomacromolecules, 2016, 17, 661
DOI: 10.1021/acs.biomac.5b01603

NMR probing of copper–amyloid β1–16 interactions and self-assembly

Punnepalli Sunanda, Srinivasarao Raghothama, Uma Maheswari Devi Palempalli and Bankala Krishnarjuna

Academia Biology, 2024, 2
DOI: 10.20935/AcadBiol7451

Sirtuin 3 attenuates amyloid-β induced neuronal hypometabolism

Junxiang Yin, Shiping Li, Megan Nielsen, Tanner Carcione, Winnie S. Liang and Jiong Shi

Aging, 2018, 10, 2874
DOI: 10.18632/aging.101592

Shear-Induced Amyloid Formation in the Brain: II. An Experimental System for Monitoring Amyloid Shear Processes and Investigating Potential Spinal Tap Problems

Conrad N. Trumbore

JAD, 2017, 59, 543
DOI: 10.3233/JAD-170259

KLVFF oligopeptide-decorated amphiphilic cyclodextrin nanomagnets for selective amyloid beta recognition and fishing

Antonino Mazzaglia, Giuseppe Di Natale, Rita Tosto, Angela Scala, Giuseppe Sortino, Anna Piperno, Maria Pia Casaletto, Alberto Riminucci, Maria Laura Giuffrida, Placido G. Mineo, Valentina Villari, Norberto Micali and Giuseppe Pappalardo

Journal of Colloid and Interface Science, 2022, 613, 814
DOI: 10.1016/j.jcis.2022.01.051

Passive Immunotherapies Targeting Amyloid Beta and Tau Oligomers in Alzheimer’s Disease

Crystal M. Vander Zanden and Eva Y. Chi

Journal of Pharmaceutical Sciences, 2020, 109, 68
DOI: 10.1016/j.xphs.2019.10.024

NMR studies of amyloid interactions

David A. Middleton

Progress in Nuclear Magnetic Resonance Spectroscopy, 2024, 144-145, 63
DOI: 10.1016/j.pnmrs.2024.07.001

Novel combination of Olesoxime/Resveratrol-encapsulated exosomes to improve cognitive function by targeting amyloid β-induced Alzheimer’s disease: investigation on in vitro and in vivo model

Zhuo Wang, Chao Gao, Lei Zhang and Rubo Sui

Inflammopharmacol, 2024, 32, 2613
DOI: 10.1007/s10787-024-01476-1

Impact of membrane curvature on amyloid aggregation

Mayu S. Terakawa, Yuxi Lin, Misaki Kinoshita, Shingo Kanemura, Dai Itoh, Toshihiko Sugiki, Masaki Okumura, Ayyalusamy Ramamoorthy and Young-Ho Lee

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1741
DOI: 10.1016/j.bbamem.2018.04.012

Strategies Employing Transition Metal Complexes To Modulate Amyloid-β Aggregation

Jong-Min Suh, Gunhee Kim, Juhye Kang and Mi Hee Lim

Inorg. Chem., 2019, 58, 8
DOI: 10.1021/acs.inorgchem.8b02813

Evidence of cadmium and mercury involvement in the Aβ42 aggregation process

Daniela Meleleo, Cesare Sblano, Maria Maddalena Storelli and Rosanna Mallamaci

Biophysical Chemistry, 2020, 266, 106453
DOI: 10.1016/j.bpc.2020.106453

Nanotechnology‐empowered therapeutics targeting neurodegenerative diseases

Zhiren Wang, Karina Marie Gonzalez, Leyla Estrella Cordova and Jianqin Lu

WIREs Nanomed Nanobiotechnol, 2023, 15
DOI: 10.1002/wnan.1907

Lipid membranes induce structural conversion from amyloid oligomers to fibrils

Lei Gu and Zhefeng Guo

Biochemical and Biophysical Research Communications, 2021, 557, 122
DOI: 10.1016/j.bbrc.2021.03.174

Selection of Membrane RNA Aptamers to Amyloid Beta Peptide: Implications for Exosome-Based Antioxidant Strategies

Teresa Janas, Karolina Sapoń, Michael H. B. Stowell and Tadeusz Janas

IJMS, 2019, 20, 299
DOI: 10.3390/ijms20020299

Chiral Plasmonic Nanochains via the Self-Assembly of Gold Nanorods and Helical Glutathione Oligomers Facilitated by Cetyltrimethylammonium Bromide Micelles

Jun Lu, Yi-Xin Chang, Ning-Ning Zhang, Ying Wei, Ai-Ju Li, Jia Tai, Yao Xue, Zhao-Yi Wang, Yang Yang, Li Zhao, Zhong-Yuan Lu and Kun Liu

ACS Nano, 2017, 11, 3463
DOI: 10.1021/acsnano.6b07697

Stabilization of a Membrane-Associated Amyloid-β Oligomer for Its Validation in Alzheimer's Disease

Montserrat Serra-Batiste, James Tolchard, Fabrice Giusti, Manuela Zoonens and Natàlia Carulla

Front. Mol. Biosci., 2018, 5
DOI: 10.3389/fmolb.2018.00038

Chemical Engineering of Self-Assembled Alzheimer’s Peptide on a Silanized Silicon Surface

Mehdi Ammar, Claire Smadja, Giang Thi Phuong Ly, Diénaba Tandjigora, Jackie Vigneron, Arnaud Etcheberry, Myriam Taverna and Elisabeth Dufour-Gergam

Langmuir, 2014, 30, 5863
DOI: 10.1021/la500695y

Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity

Oxana V. Galzitskaya, Stanislav R. Kurpe, Alexander V. Panfilov, Anna V. Glyakina, Sergei Y. Grishin, Alexey P. Kochetov, Evgeniya I. Deryusheva, Andrey V. Machulin, Sergey V. Kravchenko, Pavel A. Domnin, Alexey K. Surin, Viacheslav N. Azev and Svetlana A. Ermolaeva

IJMS, 2022, 23, 5463
DOI: 10.3390/ijms23105463

The Dynamism of Intrinsically Disordered Proteins: Binding-Induced Folding, Amyloid Formation, and Phase Separation

Samrat Mukhopadhyay

J. Phys. Chem. B, 2020, 124, 11541
DOI: 10.1021/acs.jpcb.0c07598

Reactivity of Flavonoids Containing a Catechol or Pyrogallol Moiety with Metal‐Free and Metal‐Associated Amyloid‐β

Seongmin Park, Yelim Yi and Mi Hee Lim

Bulletin Korean Chem Soc, 2021, 42, 17
DOI: 10.1002/bkcs.12172

Changes in membrane sphingolipid composition modulate dynamics and adhesion of integrin nanoclusters

Christina Eich, Carlo Manzo, Sandra de Keijzer, Gert-Jan Bakker, Inge Reinieren-Beeren, Maria F. García-Parajo and Alessandra Cambi

Sci Rep, 2016, 6
DOI: 10.1038/srep20693

A High Affinity Red Fluorescence and Colorimetric Probe for Amyloid β Aggregates

K. Rajasekhar, Nagarjun Narayanaswamy, N. Arul Murugan, Guanglin Kuang, Hans Ågren and T. Govindaraju

Sci Rep, 2016, 6
DOI: 10.1038/srep23668

Real-Time Analysis of Specific Binding between Apolipoprotein E Isoforms and Amyloid β-Peptide by Dual Polarization Interferometry

Yu Wang, Yu Xue, Shuang Wang, Jianshe Huang and Xiurong Yang

Anal. Chem., 2021, 93, 1472
DOI: 10.1021/acs.analchem.0c03542

Toxicity Inhibitors Protect Lipid Membranes from Disruption by Aβ42

Ravit Malishev, Sukhendu Nandi, Sofiya Kolusheva, Yael Levi-Kalisman, Frank-Gerrit Klärner, Thomas Schrader, Gal Bitan and Raz Jelinek

ACS Chem. Neurosci., 2015, 6, 1860
DOI: 10.1021/acschemneuro.5b00200

Structural Interaction of Apolipoprotein A-I Mimetic Peptide with Amyloid-β Generates Toxic Hetero-oligomers

Bikash Ranjan Sahoo, Michael E. Bekier, Zichen Liu, Vojc Kocman, Andrea K. Stoddard, G.M. Anantharamaiah, James Nowick, Carol A. Fierke, Yanzhuang Wang and Ayyalusamy Ramamoorthy

Journal of Molecular Biology, 2020, 432, 1020
DOI: 10.1016/j.jmb.2019.12.005

Atomic-resolution map of the interactions between an amyloid inhibitor protein and amyloid β (Aβ) peptides in the monomer and protofibril states

Moustafa Algamal, Rashik Ahmed, Naeimeh Jafari, Bilal Ahsan, Joaquin Ortega and Giuseppe Melacini

Journal of Biological Chemistry, 2017, 292, 17158
DOI: 10.1074/jbc.M117.792853

Ketones block amyloid entry and improve cognition in an Alzheimer's model

Jun Xiang Yin, Marwan Maalouf, Pengcheng Han, Minglei Zhao, Ming Gao, Turner Dharshaun, Christopher Ryan, Julian Whitelegge, Jie Wu, David Eisenberg, Eric M. Reiman, Felix E. Schweizer and Jiong Shi

Neurobiology of Aging, 2016, 39, 25
DOI: 10.1016/j.neurobiolaging.2015.11.018

In Vitro Studies on Accelerating the Degradation and Clearance of Amyloid-β Fibrils by an Antiamyloidogenic Peptide

Qian Zhang, Jing Liu, Xiaoyu Hu, Wei Wang and Zhi Yuan

ACS Macro Lett., 2015, 4, 339
DOI: 10.1021/acsmacrolett.5b00033

Mechanism of aggregation and membrane interactions of mammalian prion protein

Sabareesan Ambadi Thody, M.K. Mathew and Jayant B. Udgaonkar

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1927
DOI: 10.1016/j.bbamem.2018.02.031

Concentration Effects in Peptide–Lipid Bilayer Interactions: A Coarse-Grained Molecular Dynamics Study

Aleksandra Drajkowska and Andrzej Molski

J. Phys. Chem. B, 2026, 130, 3332
DOI: 10.1021/acs.jpcb.5c07780

Fibrillization of β‐Amyloid Peptides via Chemically Modulated Pathway

Zhong‐Hong Guo, Chien‐I Yang, Cheng‐I Ho, Shing‐Jong Huang, Yin‐Chung Chen, Hwan‐Ching Tai and Jerry Chun Chung Chan

Chemistry A European J, 2018, 24, 4939
DOI: 10.1002/chem.201706001

The Vital Role of Pink Marketing in the Creation of Women Loyalty

Aram Hanna Massoudi

Ino. j. soc. sci. econ. rev., 2020, 2, 29
DOI: 10.36923/ijsser.v2i3.74

31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition

Kazumi Haya, Yoshiteru Makino, Akie Kikuchi-Kinoshita, Izuru Kawamura and Akira Naito

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2020, 1862, 183290
DOI: 10.1016/j.bbamem.2020.183290

Tripeptide GGH as the Inhibitor of Copper-Amyloid-β-Mediated Redox Reaction and Toxicity

Xiaoyu Hu, Qian Zhang, Wei Wang, Zhi Yuan, Xushan Zhu, Bing Chen and Xingyu Chen

ACS Chem. Neurosci., 2016, 7, 1255
DOI: 10.1021/acschemneuro.6b00145

Aβ–ganglioside interactions in the pathogenesis of Alzheimer's disease

Katsumi Matsuzaki

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2020, 1862, 183233
DOI: 10.1016/j.bbamem.2020.183233

Role of Copper in the Onset of Alzheimer’s Disease Compared to Other Metals

Soghra Bagheri, Rosanna Squitti, Thomas Haertlé, Mariacristina Siotto and Ali A. Saboury

Front. Aging Neurosci., 2018, 9
DOI: 10.3389/fnagi.2017.00446

A mechanistic survey of Alzheimer's disease

Yijing Tang, Dong Zhang, Xiong Gong and Jie Zheng

Biophysical Chemistry, 2022, 281, 106735
DOI: 10.1016/j.bpc.2021.106735

Role of Cholesterol on Binding of Amyloid Fibrils to Lipid Bilayers

Cristiano L. Dias, Sharareh Jalali, Yanxing Yang and Luis Cruz

J. Phys. Chem. B, 2020, 124, 3036
DOI: 10.1021/acs.jpcb.0c00485

Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules

Hyunsung Choi, Hyun Joon Chang, Myeongsang Lee and Sungsoo Na

ChemPhysChem, 2017, 18, 817
DOI: 10.1002/cphc.201601327

Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β

Kyle J. Korshavn, Cristina Satriano, Yuxi Lin, Rongchun Zhang, Mark Dulchavsky, Anirban Bhunia, Magdalena I. Ivanova, Young-Ho Lee, Carmelo La Rosa, Mi Hee Lim and Ayyalusamy Ramamoorthy

Journal of Biological Chemistry, 2017, 292, 4638
DOI: 10.1074/jbc.M116.764092

Bacterial Model Membranes Reshape Fibrillation of a Functional Amyloid Protein

Ravit Malishev, Razan Abbasi, Raz Jelinek and Liraz Chai

Biochemistry, 2018, 57, 5230
DOI: 10.1021/acs.biochem.8b00002

Amyloid-β oligomerization monitored by single-molecule stepwise photobleaching

Lara Dresser, Patrick Hunter, Fatima Yendybayeva, Alex L. Hargreaves, Jamieson A.L. Howard, Gareth J.O. Evans, Mark C. Leake and Steven D. Quinn

Methods, 2021, 193, 80
DOI: 10.1016/j.ymeth.2020.06.007

Acidic Environment Significantly Alters Aggregation Pathway of Human Islet Amyloid Polypeptide at Negative Lipid Membrane

Jiahui Zhang, Junjun Tan, Ruoqi Pei and Shuji Ye

Langmuir, 2020, 36, 1530
DOI: 10.1021/acs.langmuir.9b03623

Lipid-Bilayer Dynamics Probed by a Carbon Dot-Phospholipid Conjugate

Sukhendu Nandi, Ravit Malishev, Susanta Kumar Bhunia, Sofiya Kolusheva, Jürgen Jopp and Raz Jelinek

Biophysical Journal, 2016, 110, 2016
DOI: 10.1016/j.bpj.2016.04.005

Exploring Peptido‐Nanocomposites in the Context of Amyloid Diseases

Nicholas Andrikopoulos, Huayuan Tang, Yue Wang, Xiufang Liang, Yuhuan Li, Thomas P. Davis and Pu Chun Ke

Angew Chem Int Ed, 2024, 63
DOI: 10.1002/anie.202309958

Insulin-degrading enzyme is activated by the C-terminus of α-synuclein

Sandeep K. Sharma, Erik Chorell and Pernilla Wittung-Stafshede

Biochemical and Biophysical Research Communications, 2015, 466, 192
DOI: 10.1016/j.bbrc.2015.09.002

Structure and Dynamics of Membrane Proteins from Solid-State NMR

Venkata S. Mandala, Jonathan K. Williams and Mei Hong

Annu. Rev. Biophys., 2018, 47, 201
DOI: 10.1146/annurev-biophys-070816-033712

Molecular Docking and Dynamic Simulation of AZD3293 and Solanezumab Effects Against BACE1 to Treat Alzheimer's Disease

Mubashir Hassan, Saba Shahzadi, Sung Y. Seo, Hany Alashwal, Nazar Zaki and Ahmed A. Moustafa

Front. Comput. Neurosci., 2018, 12
DOI: 10.3389/fncom.2018.00034

Semen‐derived amyloidogenic peptides—Key players of HIV infection

Young‐Ho Lee and Ayyalusamy Ramamoorthy

Protein Science, 2018, 27, 1151
DOI: 10.1002/pro.3395

Transmembrane clustering of short amyloid peptide fragments: A coarse grained molecular dynamics study

Aleksandra Drajkowska and Andrzej Molski

Biophysical Chemistry, 2025, 320-321, 107418
DOI: 10.1016/j.bpc.2025.107418

Electrostatic and hydrophobic interactions of lipid-associated α-synuclein: The role of a water-limited interfaces in amyloid fibrillation

Tae Su Choi, Jong Yoon Han, Chae Eun Heo, Sun Woo Lee and Hugh I. Kim

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1854
DOI: 10.1016/j.bbamem.2018.02.007

The monomers, oligomers, and fibrils of amyloid-β inhibit the activity of mitoBKCa channels by a membrane-mediated mechanism

Yevheniia Kravenska, Hanna Nieznanska, Krzysztof Nieznanski, Elena Lukyanetz, Adam Szewczyk and Piotr Koprowski

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2020, 1862, 183337
DOI: 10.1016/j.bbamem.2020.183337

Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts

Joon Lee, Young Hun Kim, Fernando T. Arce, Alan L. Gillman, Hyunbum Jang, Bruce L. Kagan, Ruth Nussinov, Jerry Yang and Ratnesh Lal

ACS Chem. Neurosci., 2017, 8, 1348
DOI: 10.1021/acschemneuro.7b00006

Ceramide: a central regulator in Alzheimer’s disease pathogenesis

Priyanka Choudhary, Shilpa Kumari, Kajal Bagri and Rahul Deshmukh

Inflammopharmacol, 2025, 33, 1775
DOI: 10.1007/s10787-025-01719-9

Synthesis and pharmacological evaluation of novel chromone derivatives as balanced multifunctional agents against Alzheimer's disease

Fan Li, Jia-Jia Wu, Jin Wang, Xue-Lian Yang, Pei Cai, Qiao-Hong Liu, Ling-Yi Kong and Xiao-Bing Wang

Bioorganic & Medicinal Chemistry, 2017, 25, 3815
DOI: 10.1016/j.bmc.2017.05.027

Interplay between Antimicrobial Peptides and Amyloid Proteins in Host Defense and Disease Modulation

Naiem Ahmad Wani, Ehud Gazit and Ayyalusamy Ramamoorthy

Langmuir, 2024, 40, 25355
DOI: 10.1021/acs.langmuir.4c03123

Modeling the Aggregation Propensity and Toxicity of Amyloid-β Variants

Manish K. Tiwari, Kasper P. Kepp and George Acquaah-Mensah

JAD, 2015, 47, 215
DOI: 10.3233/JAD-150046

Advances and Challenges in Gene Therapy for Alzheimer’s Disease

Fabiana Morroni, Antonella Caccamo, Paula I. Moreira, Jesus Avila, Daniela Galimberti, Miguel A. Pappolla, Germán Plascencia-Villa, Aaron A. Sorensen, Xiongwei Zhu and George Perry

JAD, 2024, 101, S417
DOI: 10.3233/JAD-230783

Exploring Peptido‐Nanocomposites in the Context of Amyloid Diseases

Nicholas Andrikopoulos, Huayuan Tang, Yue Wang, Xiufang Liang, Yuhuan Li, Thomas P. Davis and Pu Chun Ke

Angewandte Chemie, 2024, 136
DOI: 10.1002/ange.202309958

The on-fibrillation-pathway membrane content leakage and off-fibrillation-pathway lipid mixing induced by 40-residue β-amyloid peptides in biologically relevant model liposomes

Qinghui Cheng, Zhi-Wen Hu, Katelynne E. Doherty, Yuto J. Tobin-Miyaji and Wei Qiang

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1670
DOI: 10.1016/j.bbamem.2018.03.008

Insulin–eukaryotic model membrane interaction: Mechanistic insight of insulin fibrillation and membrane disruption

Bhisma Narayan Ratha, Minsoo Kim, Bankanidhi Sahoo, Kanchan Garai, DongKuk Lee and Anirban Bhunia

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1917
DOI: 10.1016/j.bbamem.2018.02.008

Advances in Multi-Functional Ligands and the Need for Metal-Related Pharmacology for the Management of Alzheimer Disease

Abha Sharma, Vidhu Pachauri and S. J. S. Flora

Front. Pharmacol., 2018, 9
DOI: 10.3389/fphar.2018.01247

Probing the interactions between amyloidogenic proteins and bio-membranes

Liang Ma, Xi Li, Robert B. Petersen, Anlin Peng and Kun Huang

Biophysical Chemistry, 2023, 296, 106984
DOI: 10.1016/j.bpc.2023.106984

The hazardous effects of the environmental toxic gases on amyloid beta-peptide aggregation: A theoretical perspective

Vasudevan Saranya, Pitchumani Violet Mary, Subramaniam Vijayakumar and Ramasamy Shankar

Biophysical Chemistry, 2020, 263, 106394
DOI: 10.1016/j.bpc.2020.106394

MOMD Analysis of NMR Line Shapes from Aβ-Amyloid Fibrils: A New Tool for Characterizing Molecular Environments in Protein Aggregates

Eva Meirovitch, Zhichun Liang and Jack H. Freed

J. Phys. Chem. B, 2018, 122, 4793
DOI: 10.1021/acs.jpcb.8b02181

Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy

Akira Naito, Nobuaki Matsumori and Ayyalusamy Ramamoorthy

Biochimica et Biophysica Acta (BBA) - General Subjects, 2018, 1862, 307
DOI: 10.1016/j.bbagen.2017.06.004

In-cell 31P solid-state NMR measurements of the lipid dynamics and influence of exogeneous β-amyloid peptides on live neuroblastoma neuro-2a cells

June M. Kenyaga, Sarah A. Oteino, Yan Sun and Wei Qiang

Biophysical Chemistry, 2023, 297, 107008
DOI: 10.1016/j.bpc.2023.107008

Ethanol Controls the Self-Assembly and Mesoscopic Properties of Human Insulin Amyloid Spherulites

Valeria Vetri, Federica Piccirilli, Johannes Krausser, Gianpiero Buscarino, Urszula Łapińska, Bente Vestergaard, Alessio Zaccone and Vito Foderà

J. Phys. Chem. B, 2018, 122, 3101
DOI: 10.1021/acs.jpcb.8b01779

Tuning Structures and Properties for Developing Novel Chemical Tools toward Distinct Pathogenic Elements in Alzheimer’s Disease

Jiyeon Han, Hyuck Jin Lee, Kyu Yeon Kim, Shin Jung C. Lee, Jong-Min Suh, Jaeheung Cho, Junghyun Chae and Mi Hee Lim

ACS Chem. Neurosci., 2018, 9, 800
DOI: 10.1021/acschemneuro.7b00454

Time-Dependent Lipid Dynamics, Organization and Peptide-Lipid Interaction in Phospholipid Bilayers with Incorporated β-Amyloid Oligomers

Wei Qiang, Katelynne E. Doherty, Lukas M. Klees and Yuto Tobin-Miyaji

J. Phys. Chem. Lett., 2020, 11, 8329
DOI: 10.1021/acs.jpclett.0c01967

Nutrient‐sensing amyloid metastasis

Luís Maurício T. R. Lima and Tháyna Sisnande

BioFactors, 2022, 48, 552
DOI: 10.1002/biof.1825

Toward a Soluble Model System for the Amyloid State

Nicole C. Thomas, Gail J. Bartlett, Derek N. Woolfson and Samuel H. Gellman

J. Am. Chem. Soc., 2017, 139, 16434
DOI: 10.1021/jacs.7b07225

C-terminal truncation exacerbates the aggregation and cytotoxicity of α-Synuclein: A vicious cycle in Parkinson's disease

Liang Ma, Chen Yang, Xia Zhang, Yang Li, Shun Wang, Ling Zheng and Kun Huang

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2018, 1864, 3714
DOI: 10.1016/j.bbadis.2018.10.003

Applications of scanning probe microscopy in neuroscience research

Danielle M McRae and Zoya Leonenko

J. Phys. Mater., 2024, 7, 012004
DOI: 10.1088/2515-7639/ad1d89

Uptake of raft components into amyloid β-peptide aggregates and membrane damage

Kenji Sasahara, Kenichi Morigaki and Yasuko Mori

Analytical Biochemistry, 2015, 481, 18
DOI: 10.1016/j.ab.2015.04.014

Receptor modulated assembly and drug induced disassembly of amyloid beta aggregates at asymmetric neuronal model biomembranes

Nirod Kumar Sarangi, Subrata Mondal and Tia E. Keyes

Biophysical Chemistry, 2025, 322, 107441
DOI: 10.1016/j.bpc.2025.107441

Extracellular vesicles from human pancreatic islets suppress human islet amyloid polypeptide amyloid formation

Diana Ribeiro, Istvan Horvath, Nikki Heath, Ryan Hicks, Anna Forslöw and Pernilla Wittung-Stafshede

Proc. Natl. Acad. Sci. U.S.A., 2017, 114, 11127
DOI: 10.1073/pnas.1711389114

Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases

Priscila Baltazar Gonçalves, Ana Carolina Rennó Sodero and Yraima Cordeiro

Biomolecules, 2021, 11, 767
DOI: 10.3390/biom11050767

Insights into the molecular mechanism behind solubilization of amyloidogenic polyglutamine‐containing peptides

Gunasekhar Burra and Ashwani Kumar Thakur

Peptide Science, 2019, 111
DOI: 10.1002/pep2.24094

Acetylation of Aβ40 Alters Aggregation in the Presence and Absence of Lipid Membranes

Albert W. Pilkington, Jane Schupp, Morgan Nyman, Stephen J. Valentine, David M. Smith and Justin Legleiter

ACS Chem. Neurosci., 2020, 11, 146
DOI: 10.1021/acschemneuro.9b00483

Pyrazolones Activate the Proteasome by Gating Mechanisms and Protect Neuronal Cells from β‐Amyloid Toxicity

Anna Maria Santoro, Valeria Lanza, Francesco Bellia, Diego Sbardella, Grazia R. Tundo, Alessandra Cannizzo, Giuseppe Grasso, Mariaconcetta Arizzi, Vincenzo G. Nicoletti, Stefano Alcaro, Giosuè Costa, Adriana Pietropaolo, Gaetano Malgieri, Gianluca D'Abrosca, Roberto Fattorusso, Sara García‐Viñuales, Ikhlas M. M. Ahmed, Massimiliano Coletta and Danilo Milardi

ChemMedChem, 2020, 15, 302
DOI: 10.1002/cmdc.201900612

Aβ Beyond the AD Pathology: Exploring the Structural Response of Membranes Exposed to Nascent Aβ Peptide

Valeria Rondelli, Mario Salmona, Laura Colombo, Giovanna Fragneto, Giulia C. Fadda, Laura Cantu’ and Elena Del Favero

IJMS, 2020, 21, 8295
DOI: 10.3390/ijms21218295

Opposite Roles of Cholesterol and Lanosterol in Lipid Membrane on Amyloid-Beta 42 Peptide Nucleation and Fibril Formation

Kyohei Akiho, Akane Iida-Adachi and Hideki Nabika

ACS Chem. Neurosci., 2025, 16, 195
DOI: 10.1021/acschemneuro.4c00707

Chirality‐Assisted Ring‐Like Aggregation of Aβ(1–40) at Liquid–Solid Interfaces: A Stereoselective Two‐Step Assembly Process

Guanbin Gao, Mingxi Zhang, Pei Lu, Guanlun Guo, Dong Wang and Taolei Sun

Angew Chem Int Ed, 2015, 54, 2245
DOI: 10.1002/anie.201410768

Cross-fibrillation of insulin and amyloid β on chiral surfaces: Chirality affects aggregation kinetics and cytotoxicity

Zhi Du, Yijia Guan, Chao Ding, Nan Gao, Jinsong Ren and Xiaogang Qu

Nano Res., 2018, 11, 4102
DOI: 10.1007/s12274-018-1995-y

Exploring interactions between lipids and amyloid-forming proteins: A review on applying fluorescence and NMR techniques

Ziwei Chang, Jing Deng, Weijing Zhao and Jun Yang

Chemistry and Physics of Lipids, 2021, 236, 105062
DOI: 10.1016/j.chemphyslip.2021.105062

Preparation Protocols of Aβ(1–40) Promote the Formation of Polymorphic Aggregates and Altered Interactions with Lipid Bilayers

Elizabeth A. Yates and Justin Legleiter

Biochemistry, 2014, 53, 7038
DOI: 10.1021/bi500792f

3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

Antoine Loquet, Nadia El Mammeri, Jan Stanek, Mélanie Berbon, Benjamin Bardiaux, Guido Pintacuda and Birgit Habenstein

Methods, 2018, 138-139, 26
DOI: 10.1016/j.ymeth.2018.03.014

Ordered and Disordered Segments of Amyloid-β Drive Sequential Steps of the Toxic Pathway

Barun Kumar Maity, Anand Kant Das, Simli Dey, Ullhas Kaarthi Moorthi, Amandeep Kaur, Arpan Dey, Dayana Surendran, Rucha Pandit, Mamata Kallianpur, Bappaditya Chandra, Muralidharan Chandrakesan, Senthil Arumugam and Sudipta Maiti

ACS Chem. Neurosci., 2019, 10, 2498
DOI: 10.1021/acschemneuro.9b00015

Minimalistic Principles for Designing Small Molecules with Multiple Reactivities against Pathological Factors in Dementia

Mingeun Kim, Juhye Kang, Misun Lee, Jiyeon Han, Geewoo Nam, Eunyoung Tak, Min Sun Kim, Hyuck Jin Lee, Eunju Nam, Jiyong Park, Soo Jin Oh, Ji-Yoon Lee, Joo-Yong Lee, Mu-Hyun Baik and Mi Hee Lim

J. Am. Chem. Soc., 2020, 142, 8183
DOI: 10.1021/jacs.9b13100

Self-Assembly of Ovalbumin Amyloid Pores: Effects on Membrane Permeabilization, Dipole Potential, and Bilayer Fluidity

Mily Bhattacharya and Priyanka Dogra

Langmuir, 2015, 31, 8911
DOI: 10.1021/acs.langmuir.5b02074

In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate

Jianxing Song

IJMS, 2024, 25, 12817
DOI: 10.3390/ijms252312817

The Aβ protofibril selective antibody mAb158 prevents accumulation of Aβ in astrocytes and rescues neurons from Aβ-induced cell death

Sofia Söllvander, Elisabeth Nikitidou, Linn Gallasch, Marlena Zyśk, Linda Söderberg, Dag Sehlin, Lars Lannfelt and Anna Erlandsson

J Neuroinflammation, 2018, 15
DOI: 10.1186/s12974-018-1134-4

Stabilization of Solvent to α-Sheet Structure and Conversion between α-Sheet and β-Sheet in the Fibrillation Process of Amyloid Peptide

Feihong Meng, Tong Lu and Fei Li

J. Phys. Chem. B, 2019, 123, 9576
DOI: 10.1021/acs.jpcb.9b07903

Amyloid beta cleavage by ANA‐TA9, a synthetic peptide from the ANA/BTG3 Box A region

Yusuke Hatakawa, Rina Nakamura, Motomi Konishi, Toshiyasu Sakane, Akiko Tanaka, Akira Matsuda, Motoaki Saito and Toshifumi Akizawa

A&D Transl Res & Clin Interv, 2021, 7
DOI: 10.1002/trc2.12146

Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition

Sushma Subedi, Santanu Sasidharan, Niharika Nag, Prakash Saudagar and Timir Tripathi

Molecules, 2022, 27, 1776
DOI: 10.3390/molecules27061776

On-cell nuclear magnetic resonance spectroscopy to probe cell surface interactions

Trần Thanh Tâm Phạm and Jan K. Rainey

Biochem. Cell Biol., 2021, 99, 683
DOI: 10.1139/bcb-2021-0052

Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

Julien Roche, Yang Shen, Jung Ho Lee, Jinfa Ying and Ad Bax

Biochemistry, 2016, 55, 762
DOI: 10.1021/acs.biochem.5b01259

Interaction of Membrane Vesicles with the Pseudomonas Functional Amyloid Protein FapC Facilitates Amyloid Formation

Zahra Najarzadeh, Hossein Mohammad-Beigi, Jannik Nedergaard Pedersen, Gunna Christiansen, Jan Skov Pedersen, Janni Nielsen and Daniel Otzen

SSRN Journal, 2022
DOI: 10.2139/ssrn.4177056

Nanomaterials in Alzheimer’s disease treatment: a comprehensive review

Maryam Faiyaz, Mohd. Azhardin Ganayee, Salman Akhtar, Saravanan Krishnan, Bableen Flora, Deeksha Dogra, Niraj Kumar Jha, Dinesh Kumar Chellappan, Poonam Negi, Kamal Dua, Kavindra Kumar Kesari and Piyush Kumar Gupta

Front. Biosci. (Landmark Ed), 2021, 26
DOI: 10.52586/4992

Molecular Insights into Human Serum Albumin as a Receptor of Amyloid-β in the Extracellular Region

Tae Su Choi, Hyuck Jin Lee, Jong Yoon Han, Mi Hee Lim and Hugh I. Kim

J. Am. Chem. Soc., 2017, 139, 15437
DOI: 10.1021/jacs.7b08584

Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

Dhiman Ghosh, Pradeep K. Singh, Shruti Sahay, Narendra Nath Jha, Reeba S. Jacob, Shamik Sen, Ashutosh Kumar, Roland Riek and Samir K. Maji

Sci Rep, 2015, 5
DOI: 10.1038/srep09228

Amyloid β, Tau, and α-Synuclein aggregates in the pathogenesis, prognosis, and therapeutics for neurodegenerative diseases

Urmi Sengupta and Rakez Kayed

Progress in Neurobiology, 2022, 214, 102270
DOI: 10.1016/j.pneurobio.2022.102270

Recent developments in molecular docking technology applied in food science: a review

Xuan Tao, Yukun Huang, Chong Wang, Fang Chen, Lingling Yang, Li Ling, Zhenming Che and Xianggui Chen

Int J of Food Sci Tech, 2020, 55, 33
DOI: 10.1111/ijfs.14325

Aggregation Mechanisms and Molecular Structures of Amyloid‐β in Alzheimer's Disease

Zheng Niu, Xinrui Gui, Shuang Feng and Bernd Reif

Chemistry A European J, 2024, 30
DOI: 10.1002/chem.202400277

Green tea extract EGCG plays a dual role in Aβ42 protofibril disruption and membrane protection: A molecular dynamic study

Xuewei Dong, Yiming Tang, Chendi Zhan and Guanghong Wei

Chemistry and Physics of Lipids, 2021, 234, 105024
DOI: 10.1016/j.chemphyslip.2020.105024

Effect of Tau Fragment and Membrane Interactions on Membrane Permeabilization and Peptide Aggregation

Majedul Islam, Md Raza Ul Karim, Emily Argueta, Mohammed N. Selim, Ewa P. Wojcikiewicz and Deguo Du

Membranes, 2025, 15, 208
DOI: 10.3390/membranes15070208

Thermodynamics of oligomerization and Helix-to-sheet structural transition of amyloid β-protein on anionic phospholipid vesicles

Keisuke Ikeda, Yuuki Sugiura, Hiroyuki Nakao and Minoru Nakano

Biophysical Chemistry, 2024, 310, 107248
DOI: 10.1016/j.bpc.2024.107248

Molecular Design of β‐Sheet Peptide for the Multi‐Modal Analysis of Disease

Hongyan Cao, Yunyun Wang, Yuan Gao, Xinli Deng, Yulong Cong, Ye Liu and Xingyu Jiang

Angewandte Chemie, 2019, 131, 1640
DOI: 10.1002/ange.201809716

Amyloid Fibril Formation on Neuronal Cells in the Coexistence of Aβ40 and Aβ42

Mayu Kawaguchi, Kenichi Kawano, Aoi Taniguchi, Atsushi Tanaka and Katsumi Matsuzaki

ChemBioChem, 2024, 25
DOI: 10.1002/cbic.202400603

Ultraviolet light triggers the conversion of Cu2+-bound Aβ42 aggregates into cytotoxic species in a copper chelation-independent manner

Xiongwei Dong, Zhe Zhang, Dan Zhao, Yaojing Liu, Yan Meng, Yong Zhang, Dan Zhang and Changlin Liu

Sci Rep, 2015, 5
DOI: 10.1038/srep13897

Sugar distributions on gangliosides guide the formation and stability of amyloid-β oligomers

Jhinuk Saha, Brea J. Ford, Xianjun Wang, Sydney Boyd, Sarah E. Morgan and Vijayaraghavan Rangachari

Biophysical Chemistry, 2023, 300, 107073
DOI: 10.1016/j.bpc.2023.107073

Targeting the hydrophobic region of pyroglutamate‐modified amyloid‐β by tyrocidine A prevents its nucleation–aggregation process and its “catalytic effect” on the Aβs aggregation

Wenjing Qin, Daoyuan Chen, Youqiao Wang, Ziyi Liu, Binhua Zhou, Xianzhang Bu and Gesi Wen

J Biochem & Molecular Tox, 2024, 38
DOI: 10.1002/jbt.23800

Structure of the transmembrane domain of human nicastrin-a component of γ-secretase

Yan Li, Lynette Sin Yee Liew, Qingxin Li and CongBao Kang

Sci Rep, 2016, 6
DOI: 10.1038/srep19522

Effect of packing density of lipid vesicles on the Aβ42 fibril polymorphism

Chae Eun Heo, Chae Ri Park and Hugh I. Kim

Chemistry and Physics of Lipids, 2021, 236, 105073
DOI: 10.1016/j.chemphyslip.2021.105073

Understanding familial Alzheimer's disease: The fit‐stay‐trim mechanism of γ‐secretase

Rukmankesh Mehra and Kasper Planeta Kepp

WIREs Comput Mol Sci, 2022, 12
DOI: 10.1002/wcms.1556

Peptide Self‐Assembly into Amyloid Fibrils at Hard and Soft Interfaces—From Corona Formation to Membrane Activity

Torsten John, Lisandra L. Martin and Bernd Abel

Macromolecular Bioscience, 2023, 23
DOI: 10.1002/mabi.202200576

Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils

S. R. Natesh, A. R. Hummels, J. R. Sachleben, T. R. Sosnick, K. F. Freed, J. F. Douglas, S. C. Meredith and E. J. Haddadian

The Journal of Chemical Physics, 2021, 154
DOI: 10.1063/5.0049250

Computational modelling of potent β-secretase (BACE1) inhibitors towards Alzheimer's disease treatment

Samuel C. Ugbaja, Zainab K. Sanusi, Patrick Appiah-Kubi, Monsurat M. Lawal and Hezekiel M. Kumalo

Biophysical Chemistry, 2021, 270, 106536
DOI: 10.1016/j.bpc.2020.106536

Transient dynamics of Aβ contribute to toxicity in Alzheimer’s disease

E. Hubin, N. A. J. van Nuland, K. Broersen and K. Pauwels

Cell. Mol. Life Sci., 2014, 71, 3507
DOI: 10.1007/s00018-014-1634-z

Molecular Design of β‐Sheet Peptide for the Multi‐Modal Analysis of Disease

Hongyan Cao, Yunyun Wang, Yuan Gao, Xinli Deng, Yulong Cong, Ye Liu and Xingyu Jiang

Angew Chem Int Ed, 2019, 58, 1626
DOI: 10.1002/anie.201809716

Cell size effects in the molecular dynamics of the intrinsically disordered Aβ peptide

Rukmankesh Mehra and Kasper P. Kepp

The Journal of Chemical Physics, 2019, 151
DOI: 10.1063/1.5115085

Ultrasmall Molybdenum Disulfide Quantum Dots Cage Alzheimer’s Amyloid Beta to Restore Membrane Fluidity

Yuhuan Li, Huayuan Tang, Houjuan Zhu, Aleksandr Kakinen, Di Wang, Nicholas Andrikopoulos, Yunxiang Sun, Aparna Nandakumar, Eunbi Kwak, Thomas P. Davis, David Tai Leong, Feng Ding and Pu Chun Ke

ACS Appl. Mater. Interfaces, 2021, 13, 29936
DOI: 10.1021/acsami.1c06478

Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics

Debabrata Maity

ChemMedChem, 2023, 18
DOI: 10.1002/cmdc.202200499

(Bio)chemical Strategies To Modulate Amyloid-β Self-Assembly

Sara Ayala, Pierre Genevaux, Christelle Hureau and Peter Faller

ACS Chem. Neurosci., 2019, 10, 3366
DOI: 10.1021/acschemneuro.9b00239

β-Amyloid-Acetylcholine Molecular Interaction: New Role of Cholinergic Mediators in Anti-Alzheimer Therapy?

Manuela Grimaldi, Sara Di Marino, Fulvio Florenzano, Maria Teresa Ciotta, Stefania Lucia Nori, Manuela Rodriquez, Giuseppe Sorrentino, Anna Maria D'Ursi and Mario Scrima

Future Med. Chem., 2016, 8, 1179
DOI: 10.4155/fmc-2016-0006

Interaction of Aβ1–42 Amyloids with Lipids Promotes “Off-Pathway” Oligomerization and Membrane Damage

Sarah Henry, Hélène Vignaud, Claude Bobo, Marion Decossas, Oliver Lambert, Etienne Harte, Isabel D. Alves, Christophe Cullin and Sophie Lecomte

Biomacromolecules, 2015, 16, 944
DOI: 10.1021/bm501837w

Metal binding to the amyloid-β peptides in the presence of biomembranes: potential mechanisms of cell toxicity

Sebastian K. T. S. Wärmländer, Nicklas Österlund, Cecilia Wallin, Jinming Wu, Jinghui Luo, Ann Tiiman, Jüri Jarvet and Astrid Gräslund

J Biol Inorg Chem, 2019, 24, 1189
DOI: 10.1007/s00775-019-01723-9

Application of synthetic lipid droplets in metabolic diseases

Pengxiang Zhao, Zichen Zhao, Ziwei Yu, Lupeng Chen, Yi Jin, Jian Wu and Zhuqing Ren

Clinical & Translational Med, 2023, 13
DOI: 10.1002/ctm2.1441

Development of a novel fluorescence assay for studying lipid bilayer perturbation induced by amyloidogenic peptides using cell plasma membrane vesicles

Mathew Sebastiao, Margaryta Babych, Noé Quittot, Kiran Kumar, Alexandre A. Arnold, Isabelle Marcotte and Steve Bourgault

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2023, 1865, 184118
DOI: 10.1016/j.bbamem.2022.184118

Toxic effects of endoplasmic reticulum stress transducer BBF2H7-derived small peptide fragments on neuronal cells

Koji Matsuhisa, Longjie Cai, Atsushi Saito, Fumika Sakaue, Yasunao Kamikawa, Sachiko Fujiwara, Rie Asada, Yukitsuka Kudo and Kazunori Imaizumi

Brain Research, 2020, 1749, 147139
DOI: 10.1016/j.brainres.2020.147139

Ratiometric Imaging Detection of Amyloid-β Fibrils by a Dual-Emissive Tris-Heteroleptic Ruthenium Complex

Si-Hai Wu, Junjie Ma, Hui-E. Peng, Ren-Hui Zheng, Zhe Zhang, Rong Yang, Lianhui Wang, Jieqing Liu, Jiao Mu, Meirong Liu, Zhong-Qiu Li, Zhong-Liang Gong, Jiang-Yang Shao and Yu-Wu Zhong

Inorg. Chem., 2024, 63, 17983
DOI: 10.1021/acs.inorgchem.4c02515

Engineering Amyloid Aggregation as a New Way to Eliminate Cancer Stem Cells by the Disruption of Iron Homeostasis

Hongshuang Qin, Tingting Cui, Zhenqi Liu, Ya Zhou, Jingsheng Niu, Jinsong Ren and Xiaogang Qu

Nano Lett., 2021, 21, 7379
DOI: 10.1021/acs.nanolett.1c02734

Three Structural Features of Functional Food Components and Herbal Medicine with Amyloid β42 Anti-Aggregation Properties

Kazuma Murakami and Kazuhiro Irie

Molecules, 2019, 24, 2125
DOI: 10.3390/molecules24112125

Fully Atomistic Aβ40 and Aβ42 Oligomers in Water: Observation of Porelike Conformations

Matthew J. Voelker, Bogdan Barz and Brigita Urbanc

J. Chem. Theory Comput., 2017, 13, 4567
DOI: 10.1021/acs.jctc.7b00495

Fibrillar and Nonfibrillar Amyloid Beta Structures Drive Two Modes of Membrane-Mediated Toxicity

Crystal M. Vander Zanden, Lois Wampler, Isabella Bowers, Erik B. Watkins, Jaroslaw Majewski and Eva Y. Chi

Langmuir, 2019, 35, 16024
DOI: 10.1021/acs.langmuir.9b02484

Interaction of membrane vesicles with the Pseudomonas functional amyloid protein FapC facilitates amyloid formation

Zahra Najarzadeh, Hossein Mohammad-Beigi, Jannik Nedergaard Pedersen, Gunna Christiansen, Jan Skov Pedersen, Janni Nielsen and Daniel E. Otzen

BBA Advances, 2022, 2, 100055
DOI: 10.1016/j.bbadva.2022.100055

Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid‐like aggregates in Escherichia coli

Susanna Navarro and Salvador Ventura

Biotechnology Journal, 2014, 9, 1259
DOI: 10.1002/biot.201400291

Environment-transformable sequence–structure relationship: a general mechanism for proteotoxicity

Jianxing Song

Biophys Rev, 2018, 10, 503
DOI: 10.1007/s12551-017-0369-0

Fibrillation of β amyloid peptides in the presence of phospholipid bilayers and the consequent membrane disruption

Wei Qiang, Wai-Ming Yau and Jürgen Schulte

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2015, 1848, 266
DOI: 10.1016/j.bbamem.2014.04.011

Liquid Crystal Enabled Early Stage Detection of Beta Amyloid Formation on Lipid Monolayers

Monirosadat Sadati, Aslin Izmitli Apik, Julio C. Armas‐Perez, Jose Martinez‐Gonzalez, Juan P. Hernandez‐Ortiz, Nicholas L. Abbott and Juan J. de Pablo

Adv Funct Materials, 2015, 25, 6050
DOI: 10.1002/adfm.201502830

High-Affinity Binding of Monomeric but Not Oligomeric Amyloid-β to Ganglioside GM1 Containing Nanodiscs

Maren Thomaier, Lothar Gremer, Christina Dammers, Judith Fabig, Philipp Neudecker and Dieter Willbold

Biochemistry, 2016, 55, 6662
DOI: 10.1021/acs.biochem.6b00829

Cause and consequence of Aβ – Lipid interactions in Alzheimer disease pathogenesis

Vijayaraghavan Rangachari, Dexter N. Dean, Pratip Rana, Ashwin Vaidya and Preetam Ghosh

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1652
DOI: 10.1016/j.bbamem.2018.03.004

Interfacial electrostatic charges promoted chemistry: Reactions and mechanisms

Qiangqiang Sun, Boran Xu, Jinyan Du, Yunlong Yu, Yujie Huang and Xu Deng

Advances in Colloid and Interface Science, 2025, 339, 103436
DOI: 10.1016/j.cis.2025.103436

Zinc significantly changes the aggregation pathway and the conformation of aggregates of human prion protein

Kai Pan, Chuan-Wei Yi, Jie Chen and Yi Liang

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015, 1854, 907
DOI: 10.1016/j.bbapap.2015.04.020

Physical Mechanism of Amyloid-β Peptide Chain Aggregation on Fluidic Lipid Nanotubules

Yu Geng, Tingting Huang, Wu Zhou and Lei Shen

Langmuir, 2022, 38, 5752
DOI: 10.1021/acs.langmuir.2c00357

Aβ8-20 Fragment as an Anti-Fibrillogenic and Neuroprotective Agent: Advancing toward Efficient Alzheimer’s Disease Treatment

Stefania Zimbone, Maria Laura Giuffrida, Giuseppina Sabatino, Giuseppe Di Natale, Rita Tosto, Grazia M. L. Consoli, Danilo Milardi, Giuseppe Pappalardo and Michele F.M. Sciacca

ACS Chem. Neurosci., 2023, 14, 1126
DOI: 10.1021/acschemneuro.2c00720

Responsive core-shell DNA particles trigger lipid-membrane disruption and bacteria entrapment

Michal Walczak, Ryan A. Brady, Leonardo Mancini, Claudia Contini, Roger Rubio-Sánchez, William T. Kaufhold, Pietro Cicuta and Lorenzo Di Michele

Nat Commun, 2021, 12
DOI: 10.1038/s41467-021-24989-7

Interaction between amyloidogenic proteins and biomembranes in protein misfolding diseases: Mechanisms, contributors, and therapy

Biao Cheng, Yang Li, Liang Ma, Zhuoyi Wang, Robert B. Petersen, Ling Zheng, Yuchen Chen and Kun Huang

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1876
DOI: 10.1016/j.bbamem.2018.02.013

Characterization of Uranyl (UO22+) Ion Binding to Amyloid Beta (Aβ) Peptides: Effects on Aβ Structure and Aggregation

Elina Berntsson, Faraz Vosough, Andra Noormägi, Kärt Padari, Fanny Asplund, Maciej Gielnik, Suman Paul, Jüri Jarvet, Vello Tõugu, Per M. Roos, Maciej Kozak, Astrid Gräslund, Andreas Barth, Margus Pooga, Peep Palumaa and Sebastian K. T. S. Wärmländer

ACS Chem. Neurosci., 2023, 14, 2618
DOI: 10.1021/acschemneuro.3c00130

ALS-causing profilin-1-mutant forms a non-native helical structure in membrane environments

Liangzhong Lim, Jian Kang and Jianxing Song

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2017, 1859, 2161
DOI: 10.1016/j.bbamem.2017.08.013

Linnaeite Mineral for NIR Light-Triggered Disruption of Alzheimer’s Pore-Forming Aβ Oligomers

Jinhyeong Jang and Chan Beum Park

ACS Appl. Mater. Interfaces, 2023, 15, 48
DOI: 10.1021/acsami.2c09601

Bacoside-A, an Indian Traditional-Medicine Substance, Inhibits β-Amyloid Cytotoxicity, Fibrillation, and Membrane Interactions

Ravit Malishev, Shira Shaham-Niv, Sukhendu Nandi, Sofiya Kolusheva, Ehud Gazit and Raz Jelinek

ACS Chem. Neurosci., 2017, 8, 884
DOI: 10.1021/acschemneuro.6b00438

Study of structural stability and damaging effect on membrane for four Aβ42 dimers

Wei Feng, Huimin Lei, Jiarui Si, Tao Zhang and Jie Zheng

PLoS ONE, 2017, 12, e0179147
DOI: 10.1371/journal.pone.0179147

Reciprocal Interactions between Membrane Bilayers and S. aureus PSMα3 Cross-α Amyloid Fibrils Account for Species-Specific Cytotoxicity

Ravit Malishev, Einav Tayeb-Fligelman, Shimrit David, Michael M. Meijler, Meytal Landau and Raz Jelinek

Journal of Molecular Biology, 2018, 430, 1431
DOI: 10.1016/j.jmb.2018.03.022

Changes in Adsorption, Aggregation, and Diffusion Nature of Amyloid β on a Lipid Membrane in an Open System

Akane Iida-Adachi and Hideki Nabika

Langmuir, 2025, 41, 3121
DOI: 10.1021/acs.langmuir.4c03663

Metabolic relationship between diabetes and Alzheimer's Disease affected by Cyclo(His-Pro) plus zinc treatment

Moon K. Song, David S. Bischoff, Albert M. Song, Koichi Uyemura and Dean T. Yamaguchi

BBA Clinical, 2017, 7, 41
DOI: 10.1016/j.bbacli.2016.09.003

N‐Terminal Charged Residues of Amyloid‐β Peptide Modulate Amyloidogenesis and Interaction with Lipid Membrane

Clifford Morris, Shirin Cupples, Thomas W. Kent, Esmail A. Elbassal, Ewa P. Wojcikiewicz, Peng Yi and Deguo Du

Chemistry A European J, 2018, 24, 9494
DOI: 10.1002/chem.201801805

Aβ-oligomers: A potential therapeutic target for Alzheimer's disease

Sudeshna Ghosh, Rafat Ali and Sandeep Verma

International Journal of Biological Macromolecules, 2023, 239, 124231
DOI: 10.1016/j.ijbiomac.2023.124231

α-Synuclein and neuronal membranes: Conformational flexibilities in health and disease

José Carlos Bozelli, Evelyn Kamski-Hennekam, Giuseppe Melacini and Richard M. Epand

Chemistry and Physics of Lipids, 2021, 235, 105034
DOI: 10.1016/j.chemphyslip.2020.105034

Islet amyloid polypeptide: Another key molecule in Alzheimer’s pathogenesis?

Yun Zhang and Weihong Song

Progress in Neurobiology, 2017, 153, 100
DOI: 10.1016/j.pneurobio.2017.03.001

ATP Kinetically Modulates Pathogenic Tau Fibrillations

Chae Eun Heo, Jong Yoon Han, Sungsu Lim, Jeeyoung Lee, Dongjoon Im, Min Jae Lee, Yun Kyung Kim and Hugh I. Kim

ACS Chem. Neurosci., 2020, 11, 3144
DOI: 10.1021/acschemneuro.0c00479

Molecular Dynamics Simulation of Small Molecules Interacting with Biological Membranes

Carlo Martinotti, Lanie Ruiz‐Perez, Evelyne Deplazes and Ricardo L. Mancera

ChemPhysChem, 2020, 21, 1486
DOI: 10.1002/cphc.202000219

Progress in Metal-Organic Supramolecular System Based on Subcomponent Self-Assembly

Changxing Ji, Guangxia Wang and Hua Wang

Chinese Journal of Organic Chemistry, 2021, 41, 2261
DOI: 10.6023/cjoc202012030

Functional dynamics in cyclic nucleotide signaling and amyloid inhibition

Bryan VanSchouwen, Rashik Ahmed, Julijana Milojevic and Giuseppe Melacini

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2017, 1865, 1529
DOI: 10.1016/j.bbapap.2017.09.005

The interplay between lipid and Aβ amyloid homeostasis in Alzheimer’s Disease: risk factors and therapeutic opportunities

Sara García-Viñuales, Michele F.M. Sciacca, Valeria Lanza, Anna Maria Santoro, Giulia Grasso, Grazia R. Tundo, Diego Sbardella, Massimiliano Coletta, Giuseppe Grasso, Carmelo La Rosa and Danilo Milardi

Chemistry and Physics of Lipids, 2021, 236, 105072
DOI: 10.1016/j.chemphyslip.2021.105072

Insights into the behavioral difference of water in the presence of GM1

Ipsita Basu, Moutusi Manna and Chaitali Mukhopadhyay

FEBS Letters, 2015, 589, 3887
DOI: 10.1016/j.febslet.2015.11.014

Assessing Glycosphingolipid Profiles in Human Health and Disease Using Non-Imaging MALDI Mass Spectrometry

Cristina Novaconi, Robert Onulov, Alina Serb, Eugen Sisu, Nicolae Dinca, Mihai-Cosmin Pascariu and Marius Georgescu

Applied Sciences, 2023, 13, 9922
DOI: 10.3390/app13179922

Inactivation of Parathyroid Hormone: Perspectives of Drug Discovery to Combating Hyperparathyroidism

Amit Kumar and Jochen Balbach

CMP, 2022, 15, 292
DOI: 10.2174/1874467214666210126112839

An O-glycopeptide participates in the formation of distinct Aβ42 fibril structures and attenuates Aβ42 neurotoxicity

Qijia Wei, Dangliang Liu, Wencheng Xia, Fengzhang Wang, Lu Huang, Jun Zhang, Xiaoya Wang, Zhongxin Xu, Changdong He, Wenzhe Li, Xiaomeng Shi, Chu Wang, Yuan Liu, Cong Liu and Suwei Dong

Nat Commun, 2025, 16
DOI: 10.1038/s41467-025-60978-w

Conformational changes of Aβ (1–42) monomers in different solvents

Myeongsang Lee, Hyun Joon Chang, Jung Yeon Park, Joonha Shin, Jong Woo Park, Jee Woo Choi, Jae In Kim and Sungsoo Na

Journal of Molecular Graphics and Modelling, 2016, 65, 8
DOI: 10.1016/j.jmgm.2016.02.003

Dissection of the key steps of amyloid-β peptide 1–40 fibrillogenesis

José P. Leite, Ana Gimeno, Pablo Taboada, Jesús J. Jiménez-Barbero and Luís Gales

International Journal of Biological Macromolecules, 2020, 164, 2240
DOI: 10.1016/j.ijbiomac.2020.08.023

Inhibiting Aggregation of β‐Amyloid by Folded and Unfolded Forms of Fimbrial Protein of Gram‐Negative Bacteria

Keisuke Yamamoto, Misa Oyaizu, Tsuyoshi Takahashi, Yoshihito Watanabe and Osami Shoji

ChemistrySelect, 2017, 2, 9058
DOI: 10.1002/slct.201700658

The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide aggregation in membrane-mimetic environments

Sylwia Król, Nicklas Österlund, Faraz Vosough, Jüri Jarvet, Sebastian Wärmländer, Andreas Barth, Leopold L. Ilag, Mazin Magzoub, Astrid Gräslund and Cecilia Mörman

iScience, 2021, 24, 102852
DOI: 10.1016/j.isci.2021.102852

Dynamic membrane interaction and amyloid fibril formation of glucagon, melittin and human calcitonin

Akira Naito and Izuru Kawamura

Biophysical Chemistry, 2023, 298, 107025
DOI: 10.1016/j.bpc.2023.107025

Exploring the binding kinetics and behaviors of self-aggregated beta-amyloid oligomers to phase-separated lipid rafts with or without ganglioside-clusters

Thuong Pham and Kwan H. Cheng

Biophysical Chemistry, 2022, 290, 106874
DOI: 10.1016/j.bpc.2022.106874

Enhanced optical asymmetry in supramolecular chiroplasmonic assemblies with long-range order

Jun Lu, Yao Xue, Kalil Bernardino, Ning-Ning Zhang, Weverson R. Gomes, Naomi S. Ramesar, Shuhan Liu, Zheng Hu, Tianmeng Sun, Andre Farias de Moura, Nicholas A. Kotov and Kun Liu

Science, 2021, 371, 1368
DOI: 10.1126/science.abd8576

Effect of phospholipid liposomes on prion fragment (106–128) amyloid formation

Deepika Regmi, Fengyun Shen, Aleksander Stanic, Majedul Islam and Deguo Du

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2023, 1865, 184199
DOI: 10.1016/j.bbamem.2023.184199

Structure Analysis of Amyloid Aggregates at Lipid Bilayers by Supercritical Angle Raman Microscopy

Valentin Dubois, Diana Serrano, Xiaotian Zhang and Stefan Seeger

Anal. Chem., 2020, 92, 4963
DOI: 10.1021/acs.analchem.9b05092

Early Divergence in Misfolding Pathways of Amyloid‐Beta Peptides

Salvatore Mamone, Stefan Glöggler, Stefan Becker and Nasrollah Rezaei‐Ghaleh

ChemPhysChem, 2021, 22, 2158
DOI: 10.1002/cphc.202100542

Non-micellar ganglioside GM1 induces an instantaneous conformational change in Aβ42 leading to the modulation of the peptide amyloid-fibril pathway

Manjeet Kumar, Magdalena I. Ivanova and Ayyalusamy Ramamoorthy

Biophysical Chemistry, 2023, 301, 107091
DOI: 10.1016/j.bpc.2023.107091

Ion channel formation by N-terminally truncated Aβ (4–42): relevance for the pathogenesis of Alzheimer's disease

Abhijith G Karkisaval, Agueda Rostagno, Rustam Azimov, Deependra K Ban, Jorge Ghiso, Bruce L. Kagan and Ratnesh Lal

Nanomedicine: Nanotechnology, Biology and Medicine, 2020, 29, 102235
DOI: 10.1016/j.nano.2020.102235

Membrane Interactions Accelerate the Self-Aggregation of Huntingtin Exon 1 Fragments in a Polyglutamine Length-Dependent Manner

Arnaud Marquette, Christopher Aisenbrey and Burkhard Bechinger

IJMS, 2021, 22, 6725
DOI: 10.3390/ijms22136725

Protein aggregation and its affecting mechanisms in neurodegenerative diseases

Junyun Wu, Jianan Wu, Tao Chen, Jing Cai and Reng Ren

Neurochemistry International, 2024, 180, 105880
DOI: 10.1016/j.neuint.2024.105880

Structures and dynamics of β-barrel oligomer intermediates of amyloid-beta16-22 aggregation

Xinwei Ge, Yunxiang Sun and Feng Ding

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1687
DOI: 10.1016/j.bbamem.2018.03.011

Plasmon-Enhanced Fluorescence Based on Gold Nanobipyramids with PEG-Controlled Distance for Near-Infrared and Visual Analysis of Amyloid-β Aggregation

Wen Sun, Jingtian Yu, Xiaoyan Liang, Rong Xu, Xiangyuan Yin, Baoxing Shen and Yaqiong Yang

ACS Appl. Mater. Interfaces, 2025, 17, 3941
DOI: 10.1021/acsami.4c18393

Aβ42/Aβ40 Ratios of Presenilin 1 Mutations Correlate with Clinical Onset of Alzheimer’s Disease

Ning Tang and Kasper P. Kepp

Journal of Alzheimer’s Disease, 2018, 66, 939
DOI: 10.3233/JAD-180829

Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes

Maria Ylenia Farrugia, Mario Caruana, Stephanie Ghio, Angelique Camilleri, Claude Farrugia, Ruben J. Cauchi, Sara Cappelli, Fabrizio Chiti and Neville Vassallo

Sci Rep, 2020, 10
DOI: 10.1038/s41598-020-74841-z

Formaldehyde‐Crosslinked Nontoxic Aβ Monomers to Form Toxic Aβ Dimers and Aggregates: Pathogenicity and Therapeutic Perspectives

Hang Zhao, Xuerong Huang and Zhiqian Tong

ChemMedChem, 2021, 16, 3376
DOI: 10.1002/cmdc.202100428

Melittin disruption of raft and non-raft-forming biomimetic membranes: A study by quartz crystal microbalance with dissipation monitoring

P. Losada-Pérez, M. Khorshid, C. Hermans, T. Robijns, M. Peeters, K.L. Jiménez-Monroy, L.T.N. Truong and P. Wagner

Colloids and Surfaces B: Biointerfaces, 2014, 123, 938
DOI: 10.1016/j.colsurfb.2014.10.048

Insights into the aggregation mechanism of Aβ(25–40)

Jian Xiong and Renee D. JiJi

Biophysical Chemistry, 2017, 220, 42
DOI: 10.1016/j.bpc.2016.11.003

Synthesis and in vitro quantification of amyloid fibrils by barbituric and thiobarbituric acid-based chromene derivatives

Seyyed Abolghasem Ghadami, Setayesh Shevidi, Leila Hosseinzadeh and Hadi Adibi

Biophysical Chemistry, 2021, 269, 106522
DOI: 10.1016/j.bpc.2020.106522

Tipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular Interfaces

Cahit Dalgicdir, Christoph Globisch, Christine Peter, Mehmet Sayar and Avner Schlessinger

PLoS Comput Biol, 2015, 11, e1004328
DOI: 10.1371/journal.pcbi.1004328

Aβ Amyloid Fibers Drastically Alter the Topography and Mechanical Properties of Lipid Membranes

Alain Bolaño Alvarez, Pablo E. A. Rodríguez, Gerardo D. Fidelio and Benjamín Caruso

Langmuir, 2023, 39, 18923
DOI: 10.1021/acs.langmuir.3c02831

Synthesis and Characterization of Propeller- and Parallel-Type Full-Length Amyloid β40 Trimer Models

Ayumi Uchino, Yumi Irie, Chihiro Tsukano, Taiji Kawase, Kenji Hirose, Yusuke Kageyama, Ikuo Tooyama, Ryo C. Yanagita and Kazuhiro Irie

ACS Chem. Neurosci., 2022, 13, 2517
DOI: 10.1021/acschemneuro.2c00363

End Capping Alters the Structural Characteristics and Mechanical Properties of Transthyretin (105–115) Amyloid Protofibrils

Myeongsang Lee and Sungsoo Na

ChemPhysChem, 2016, 17, 425
DOI: 10.1002/cphc.201500945

Size-Dependent Interaction of Amyloid β Oligomers with Brain Total Lipid Extract Bilayer—Fibrillation Versus Membrane Destruction

Dusan Mrdenovic, Marta Majewska, Izabela S. Pieta, Piotr Bernatowicz, Robert Nowakowski, Wlodzimierz Kutner, Jacek Lipkowski and Piotr Pieta

Langmuir, 2019, 35, 11940
DOI: 10.1021/acs.langmuir.9b01645

NMR-based site-resolved profiling of β-amyloid misfolding reveals structural transitions from pathologically relevant spherical oligomer to fibril

Yiling Xiao, Isamu Matsuda, Masafumi Inoue, Tomoya Sasahara, Minako Hoshi and Yoshitaka Ishii

Journal of Biological Chemistry, 2020, 295, 458
DOI: 10.1074/jbc.RA119.008522

Binary Structure of Amyloid Beta Oligomers Revealed by Dual Recognition Mapping

Jihyun Yoon, Youngkyu Kim and Joon Won Park

Anal. Chem., 2019, 91, 8422
DOI: 10.1021/acs.analchem.9b01316

Inhibition of BACE1 and amyloid β aggregation by polyketide from Streptomyces sp.

Masashi Yokoya, Keiyo Nakai, Miki Kawashima, Sanae Kurakado, Natchanun Sirimangkalakitti, Yoshihiro Kino, Takashi Sugita, Shinya Kimura, Masamichi Yamanaka and Naoki Saito

Chem Biol Drug Des, 2022, 99, 264
DOI: 10.1111/cbdd.13980

Influence of sequence and lipid type on membrane perturbation by human and rat amyloid β-peptide (1–42)

Anne M. Brown and David R. Bevan

Archives of Biochemistry and Biophysics, 2017, 614, 1
DOI: 10.1016/j.abb.2016.11.006

Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner

Sandeep K. Sharma, Erik Chorell, Pär Steneberg, Emma Vernersson-Lindahl, Helena Edlund and Pernilla Wittung-Stafshede

Sci Rep, 2015, 5
DOI: 10.1038/srep12531

Length‐Dependent Manifestation of Vibration Modes Regulates a Specific Intermediate Morphology of Aβ17‐42 in Different Environments

Hyunsung Choi, Taeyoung Yoon and Sungsoo Na

ChemPhysChem, 2018, 19, 1643
DOI: 10.1002/cphc.201800010

Aggregation kinetics in the presence of brain lipids of Aβ(1–40) cleaved from a soluble fusion protein

Miriam A. Kael, Daniel K. Weber, Frances Separovic and Marc-Antoine Sani

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1681
DOI: 10.1016/j.bbamem.2018.03.005

Curcumin Binding to Beta Amyloid: A Computational Study

Praveen P. N. Rao, Tarek Mohamed, Karan Teckwani and Gary Tin

Chem Biol Drug Des, 2015, 86, 813
DOI: 10.1111/cbdd.12552

Unilamellar Vesicles from Amphiphilic Graphene Quantum Dots

Sukhendu Nandi, Sofiya Kolusheva, Ravit Malishev, Alexander Trachtenberg, T. P. Vinod and Raz Jelinek

Chemistry A European J, 2015, 21, 7755
DOI: 10.1002/chem.201406170

Inactivation of seeding activity of amyloid β‐protein aggregates in vitro

Hiroto Nakano, Tsuyoshi Hamaguchi, Tokuhei Ikeda, Takahiro Watanabe‐Nakayama, Kenjiro Ono and Masahito Yamada

Journal of Neurochemistry, 2022, 160, 499
DOI: 10.1111/jnc.15563

Effect of a Short Peptide with Alternating L- and D-Amino Acid on the Aggregation and Membrane Damage of hIAPP

Feihong Meng, Yajie Wang, Tong Lu, Chunyu Wang and Fei Li

Chem. Res. Chin. Univ., 2021, 37, 787
DOI: 10.1007/s40242-021-0386-1

Strikingly different effects of cholesterol and 7-ketocholesterol on lipid bilayer-mediated aggregation of amyloid beta (1-42)

Huong T.T. Phan, Naofumi Shimokawa, Neha Sharma, Masahiro Takagi and Mun'delanji C. Vestergaard

Biochemistry and Biophysics Reports, 2018, 14, 98
DOI: 10.1016/j.bbrep.2018.04.007

Characterization of a Conformation-Restricted Amyloid β Peptide and Immunoreactivity of Its Antibody in Human AD brain

Yusuke Kageyama, Yumi Irie, Yuka Matsushima, Tatsuya Segawa, Jean-Pierre Bellier, Kumi Hidaka, Hiroshi Sugiyama, Daita Kaneda, Yoshio Hashizume, Hiroyasu Akatsu, Kunio Miki, Akiko Kita, Douglas G. Walker, Kazuhiro Irie and Ikuo Tooyama

ACS Chem. Neurosci., 2021, 12, 3418
DOI: 10.1021/acschemneuro.1c00416

Globular-shaped Aβ oligomers have diverse mechanisms for promoting Aβ aggregations with the facilitation of fibril elongation

Hiroto Nakano, Sadao Hikishima, Makoto Mori, Jota Minamikawa, Daiki Muramatsu, Yasuhiro Sakashita, Tokuhei Ikeda, Moeko Noguchi-Shinohara, David B. Teplow and Kenjiro Ono

Neurobiology of Disease, 2025, 205, 106775
DOI: 10.1016/j.nbd.2024.106775

Toxic mechanisms of amyloid oligomers and therapeutic strategies

Magdalena I. Ivanova, Carmelo La Rosa and Ayyalusamy Ramamoorthy

Protein Science, 2026, 35
DOI: 10.1002/pro.70519

Scavenging amyloid oligomers from neurons with silica nanobowls: Implications for amyloid diseases

Vrinda Sant, Madhura Som, Abhijith G. Karkisaval, Parker Carnahan and Ratnesh Lal

Biophysical Journal, 2021, 120, 3329
DOI: 10.1016/j.bpj.2021.07.002

Membrane Binding and Pore Formation by a Cytotoxic Fragment of Amyloid β Peptide

Nabin Kandel, Tianyu Zheng, Qun Huo and Suren A. Tatulian

J. Phys. Chem. B, 2017, 121, 10293
DOI: 10.1021/acs.jpcb.7b07002

Multifunctional coumarin derivatives: Monoamine oxidase B (MAO-B) inhibition, anti-β-amyloid (Aβ) aggregation and metal chelation properties against Alzheimer’s disease

Ming Huang, Sai-Sai Xie, Neng Jiang, Jin-Shuai Lan, Ling-Yi Kong and Xiao-Bing Wang

Bioorganic & Medicinal Chemistry Letters, 2015, 25, 508
DOI: 10.1016/j.bmcl.2014.12.034

Toxic Amyloid Tape: A Novel Mixed Antiparallel/Parallel β-Sheet Structure Formed by Amyloid β-Protein on GM1 Clusters

Yuki Okada, Kaori Okubo, Keisuke Ikeda, Yoshiaki Yano, Masaru Hoshino, Yoshio Hayashi, Yoshiaki Kiso, Hikari Itoh-Watanabe, Akira Naito and Katsumi Matsuzaki

ACS Chem. Neurosci., 2019, 10, 563
DOI: 10.1021/acschemneuro.8b00424

CuII Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function

Ewelina Stefaniak and Wojciech Bal

Inorg. Chem., 2019, 58, 13561
DOI: 10.1021/acs.inorgchem.9b01399

Molecular Mechanism for the Suppression of Alpha Synuclein Membrane Toxicity by an Unconventional Extracellular Chaperone

Rashik Ahmed, Jinfeng Huang, Daniel K. Weber, Tata Gopinath, Gianluigi Veglia, Madoka Akimoto, Adree Khondker, Maikel C. Rheinstädter, Vincent Huynh, Ryan G. Wylie, José C. Bozelli, Richard M. Epand and Giuseppe Melacini

J. Am. Chem. Soc., 2020
DOI: 10.1021/jacs.0c01894

HuM195 and its single-chain variable fragment increase Aβ phagocytosis in microglia via elimination of CD33 inhibitory signaling

Eitan Wong, Manish Malviya, Tanya Jain, George P. Liao, Zoe Kehs, Jerry C. Chang, Lorenz Studer, David A. Scheinberg and Yue-Ming Li

Mol Psychiatry, 2024, 29, 2084
DOI: 10.1038/s41380-024-02474-z

Inhibiting Aβ toxicity in Alzheimer's disease by a pyridine amine derivative

Zhenzhu Zhu, Tao Yang, Lei Zhang, Lulu Liu, Enmao Yin, Changli Zhang, Zijian Guo, Chen Xu and Xiaoyong Wang

European Journal of Medicinal Chemistry, 2019, 168, 330
DOI: 10.1016/j.ejmech.2019.02.052

Alzheimer’s disease: How metal ions define β-amyloid function

Kasper P. Kepp

Coordination Chemistry Reviews, 2017, 351, 127
DOI: 10.1016/j.ccr.2017.05.007

Ion mobility-mass spectrometry and orthogonal gas-phase techniques to study amyloid formation and inhibition

Waldemar Hoffmann, Gert von Helden and Kevin Pagel

Current Opinion in Structural Biology, 2017, 46, 7
DOI: 10.1016/j.sbi.2017.03.002

Amyloid cascade in Alzheimer's disease: Recent advances in medicinal chemistry

Tarek Mohamed, Arash Shakeri and Praveen P.N. Rao

European Journal of Medicinal Chemistry, 2016, 113, 258
DOI: 10.1016/j.ejmech.2016.02.049

Nonequilibrium molecular dynamics simulations of infrared laser-induced dissociation of a tetrameric Aβ42 β-barrel in a neuronal membrane model

Viet Hoang Man, Junmei Wang, Philippe Derreumaux and Phuong H. Nguyen

Chemistry and Physics of Lipids, 2021, 234, 105030
DOI: 10.1016/j.chemphyslip.2020.105030

Effects of Familial Alzheimer’s Disease Mutations on the Assembly of a β-Hairpin Peptide Derived from Aβ16–36

Kate J. McKnelly, Adam G. Kreutzer, William J. Howitz, Katelyn Haduong, Stan Yoo, Candace Hart and James S. Nowick

Biochemistry, 2022, 61, 446
DOI: 10.1021/acs.biochem.1c00664

Aggregation of Beta‐Amyloid Peptides Proximal to Zwitterionic Lipid Bilayers

Chien‐I Yang, Brook N. F. Tsai, Shing‐Jong Huang, Ting‐Yu Wang, Hwan‐Ching Tai and Jerry C. C. Chan

Chemistry An Asian Journal, 2015, 10, 1967
DOI: 10.1002/asia.201500482

Alzheimer’s Disease as a Membrane Disorder: Spatial Cross-Talk Among Beta-Amyloid Peptides, Nicotinic Acetylcholine Receptors and Lipid Rafts

Camila Fabiani and Silvia S. Antollini

Front. Cell. Neurosci., 2019, 13
DOI: 10.3389/fncel.2019.00309

Molecular insight into cross-interaction between amyloid β isoforms and its effect on aggregation pathways

Li Wang, Sanghwan Park, Jae Hong Choi, Chang Young Lee, Kilho Eom and Taeyun Kwon

Journal of Biomolecular Structure and Dynamics, 2025, 43, 11005
DOI: 10.1080/07391102.2025.2475221

Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1–40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol

Durgesh K. Rai, Veerendra K. Sharma, Divina Anunciado, Hugh O’Neill, Eugene Mamontov, Volker Urban, William T. Heller and Shuo Qian

Sci Rep, 2016, 6
DOI: 10.1038/srep30983

Membrane Determinants Affect Fibrillation Processes of β-Sheet Charged Peptides

Elad Arad, Ravit Malishev, Hanna Rapaport and Raz Jelinek

Biomacromolecules, 2018, 19, 307
DOI: 10.1021/acs.biomac.7b01318

Physiologically-relevant levels of sphingomyelin, but not GM1, induces a β-sheet-rich structure in the amyloid-β(1-42) monomer

Michael C. Owen, Waldemar Kulig, Chetan Poojari, Tomasz Rog and Birgit Strodel

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2018, 1860, 1709
DOI: 10.1016/j.bbamem.2018.03.026

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

Phuong H. Nguyen, Ayyalusamy Ramamoorthy, Bikash R. Sahoo, Jie Zheng, Peter Faller, John E. Straub, Laura Dominguez, Joan-Emma Shea, Nikolay V. Dokholyan, Alfonso De Simone, Buyong Ma, Ruth Nussinov, Saeed Najafi, Son Tung Ngo, Antoine Loquet, Mara Chiricotto, Pritam Ganguly, James McCarty, Mai Suan Li, Carol Hall, Yiming Wang, Yifat Miller, Simone Melchionna, Birgit Habenstein, Stepan Timr, Jiaxing Chen, Brianna Hnath, Birgit Strodel, Rakez Kayed, Sylvain Lesné, Guanghong Wei, Fabio Sterpone, Andrew J. Doig and Philippe Derreumaux

Chem. Rev., 2021, 121, 2545
DOI: 10.1021/acs.chemrev.0c01122

Small Liposomes Accelerate the Fibrillation of Amyloid β (1–40)

Mayu S. Terakawa, Hisashi Yagi, Masayuki Adachi, Young-Ho Lee and Yuji Goto

Journal of Biological Chemistry, 2015, 290, 815
DOI: 10.1074/jbc.M114.592527

Structural Changes of Amyloid β-Protein Fibrils on Neuronal Cells

Yuto Kado, Kenichi Kawano, Marie Nishikawa, Atsushi Tanaka, Yoshiaki Yano, Masaru Hoshino and Katsumi Matsuzaki

ACS Chem. Neurosci., 2025, 16, 2387
DOI: 10.1021/acschemneuro.5c00064

Pathological concentration of zinc dramatically accelerates abnormal aggregation of full-length human Tau and thereby significantly increases Tau toxicity in neuronal cells

Ji-Ying Hu, De-Lin Zhang, Xiao-Ling Liu, Xue-Shou Li, Xiao-Qing Cheng, Jie Chen, Hai-Ning Du and Yi Liang

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2017, 1863, 414
DOI: 10.1016/j.bbadis.2016.11.022

Levels of Organochlorine Pesticides Are Associated with Amyloid Aggregation in Apex Avian Brains

Kelly A. Heys, Richard F. Shore, M. Glória Pereira and Francis L. Martin

Environ. Sci. Technol., 2017, 51, 8672
DOI: 10.1021/acs.est.7b00840

Morphology‐Specific Inhibition of β‐Amyloid Aggregates by 17β‐Hydroxysteroid Dehydrogenase Type 10

Laura Aitken, Steven D. Quinn, Cibran Perez‐Gonzalez, Ifor D. W. Samuel, J. Carlos Penedo and Frank J. Gunn‐Moore

ChemBioChem, 2016, 17, 1029
DOI: 10.1002/cbic.201600081

Catalytides derived from the Box A region in the ANA/BTG3 protein cleave amyloid-β fragment peptide

Yusuke Hatakawa, Rina Nakamura, Motomi Konishi, Toshiyasu Sakane, Motoaki Saito and Toshifumi Akizawa

Heliyon, 2019, 5, e02454
DOI: 10.1016/j.heliyon.2019.e02454

Cell-Size Space Regulates the Behavior of Confined Polymers: From Nano- and Micromaterials Science to Biology

Miho Yanagisawa, Chiho Watanabe, Natsuhiko Yoshinaga and Kei Fujiwara

Langmuir, 2022, 38, 11811
DOI: 10.1021/acs.langmuir.2c01397

New insights into the molecular mechanisms of biomembrane structural changes and interactions by optical biosensor technology

Tzong-Hsien Lee, Daniel J. Hirst and Marie-Isabel Aguilar

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2015, 1848, 1868
DOI: 10.1016/j.bbamem.2015.05.012

Study on the structure and membrane disruption of the peptide oligomers constructed by hIAPP18–27 peptide and its d,l-alternating isomer

Shuang Wang, Feihong Meng, Ruijie Hao, Chunyu Wang and Fei Li

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2020, 1862, 183108
DOI: 10.1016/j.bbamem.2019.183108

Pore Formation Mechanism of A-Beta Peptide on the Fluid Membrane: A Combined Coarse-Grained and All-Atomic Model

Yuxi Dai, Zhexing Xie and Lijun Liang

Molecules, 2022, 27, 3924
DOI: 10.3390/molecules27123924

Ganglioside-Enriched Phospholipid Vesicles Induce Cooperative Aβ Oligomerization and Membrane Disruption

Jhinuk Saha, Priyankar Bose, Shailendra Dhakal, Preetam Ghosh and Vijayaraghavan Rangachari

Biochemistry, 2022, 61, 2206
DOI: 10.1021/acs.biochem.2c00495

A rhein-huprine hybrid protects erythrocyte membrane integrity against Alzheimer’s disease related Aβ(1-42) peptide

Pablo Zambrano, Malgorzata Jemiola-Rzeminska, Diego Muñoz-Torrero, Mario Suwalsky and Kazimierz Strzalka

Biophysical Chemistry, 2023, 300, 107061
DOI: 10.1016/j.bpc.2023.107061