Teaching an old scaffold new recognition tricks: oligopyrrolamide antagonists of IAPP aggregation


Sunil Kumar, Maria C. Vogel and Andrew D. Hamilton
Org. Biomol. Chem., 2018,16, 733-741
From themed collection: Chemical biology in OBC

Abstract

An oligopyrrolamide was identified as a potent antagonist of the aggregation of IAPP, a process associated with type 2 diabetes.


Synthesis and characterization of water-soluble macrocyclic peptides stabilizing protein α-turn


Lei Wang, Pascale Coric, Kexin Zhu, Wang-Qing Liu, Michel Vidal, Serge Bouaziz and Sylvain Broussy
Org. Biomol. Chem., 2018,16, 459-471
From themed collection: Chemical biology in OBC

Abstract

Macrocyclic peptides mimic tight “non-classical” α-turn type II-αLS found in proteins, as shown by spectroscopic and computational analysis of their equilibrating conformations.


Stereocontrolled glycoside synthesis by activation of glycosyl sulfone donors with scandium(III) triflate


Amandine Xolin, Romain Losa, Aicha Kaid, Cédric Tresse, Jean-Marie Beau, François-Didier Boyer and Stéphanie Norsikian
Org. Biomol. Chem., 2018,16, 325-335
From themed collection: Chemical biology in OBC

Abstract

Activation of armed glycosyl sulfone donors, using scandium(III) triflate under microwave irradiation, provides a selective preparation of α-mannosides.


Synthesis and structural investigation of a series of mannose-containing oligosaccharides using mass spectrometry


S. Daikoku, R. Pendrill, Y. Kanie, Y. Ito, G. Widmalm and O. Kanie
Org. Biomol. Chem., 2018,16, 228-238
From themed collection: Chemical biology in OBC

Abstract

Gas-phase collision-induced dissociation and acid hydrolysis of mannose-containing oligosaccharides were performed, which revealed the reactivity order of linkage isomers.


Side chain-specific 11/9-helix propensity of α/β-peptides with alternating residue types


Jaeyeon Lee, Jihyun Shim, Philjae Kang, Moon-Gun Choi and Soo Hyuk Choi
Org. Biomol. Chem., 2018,16, 433-438
From themed collection: Chemical biology in OBC

Abstract

The 11/9-helix propensity of α/β-peptides is dependent on a specific side chain group of α- or β3-residue.


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Predicting allosteric mutants that increase activity of a major antibiotic resistance enzyme


M. J. Latallo, G. A. Cortina, S. Faham, R. K. Nakamoto and P. M. Kasson
Chem. Sci., 2017,8, 6484-6492

Abstract

Allosteric mutations increasing kcat in a beta lactamase act by changing conformational ensembles of active-site residues identified by machine learning.


Nanowire sensors monitor bacterial growth kinetics and response to antibiotics


B. Ibarlucea, T. Rim, C. K. Baek, J. A. G. M. de Visser, L. Baraban and G. Cuniberti
Lab Chip, 2017,17, 4283-4293

Abstract

We monitor bacterial growth kinetics and response to bactericidal and bacteriostatic antibiotics using silicon nanowire transistors.


Linear humidity response of carbon dot-modified molybdenum disulfide


Guili He, Da Huang, Zhi Yang, Yutong Han, Jun Hu, Nantao Hu, Yanjie Su, Zhihua Zhou, Yafei Zhang and Yan Zhang
Phys. Chem. Chem. Phys., 2018,20, 4083-4091

Abstract

The humidity performance of MoS2 modified by carbon dots has been significantly improved due to the increased surface area and the increased activity sites.


A multifunnel energy landscape encodes the competing α-helix and β-hairpin conformations for a designed peptide


Debayan Chakraborty, Yassmine Chebaro and David J. Wales
Phys. Chem. Chem. Phys., 2020,22, 1359-1370

Abstract

The propensities to form different secondary structures are encoded in the multifunnel nature of the underlying free energy landscape, and conformational switching between such structures is a key element of protein folding and aggregation.


Conformational stabilization of a β-hairpin through a triazole–tryptophan interaction


Donatella Diana, Claudia Di Salvo, Veronica Celentano, Lucia De Rosa, Alessandra Romanelli, Roberto Fattorusso and Luca D. D'Andrea
Org. Biomol. Chem., 2018,16, 787-795

Abstract

Triazole and indole rings stabilize a β-hairpin conformation through an aromatic–aromatic interaction.


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