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Themed collection Biophysical studies on protein misfolding and amyloid diseases

13 items
Perspective

Alzheimer's disease: which type of amyloid-preventing drug agents to employ?

The amyloid hypothesis and toxic ion channel formation in Alzheimer's disease.

Graphical abstract: Alzheimer's disease: which type of amyloid-preventing drug agents to employ?
Open Access Paper

Determination of orientations of aromatic groups in self-assembled peptide fibrils by polarised Raman spectroscopy

In this paper we describe a novel combination of Raman spectroscopy, isotope editing and X-ray scattering as a powerful approach to give detailed structural information on aromatic side chains in peptide fibrils.

Graphical abstract: Determination of orientations of aromatic groups in self-assembled peptide fibrils by polarised Raman spectroscopy
Paper

Copper(II)–human amylin complex protects pancreatic cells from amylin toxicity

Cu2+ mitigates aggregation and toxicity of human amylin by stabilizing the peptide in its native, random-coil conformational state.

Graphical abstract: Copper(ii)–human amylin complex protects pancreatic cells from amylin toxicity
Paper

Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure

The amyloid β-peptide (Aβ) is the major structural component of amyloid fibrils in the plaques of brains of Alzheimer's disease patients.

Graphical abstract: Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure
Paper

Stereochemical effects on the aggregation and biological properties of the fibril-forming peptide [KIGAKI]3 in membranes

Conformational equilibria of [KIGAKI]3.

Graphical abstract: Stereochemical effects on the aggregation and biological properties of the fibril-forming peptide [KIGAKI]3 in membranes
Paper

Amyloid-β–neuropeptide interactions assessed by ion mobility-mass spectrometry

Small neuropeptides can bind to amyloid-β and modulate their aggregation in vitro.

Graphical abstract: Amyloid-β–neuropeptide interactions assessed by ion mobility-mass spectrometry
Paper

Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: towards a unifying description of conformational transitions, oligomerization and membrane damage

Twisted arrangements of α-helical Aβ (1–40) peptides are spontaneously assembled in membranes and act as mechanical stressors of the bilayer.

Graphical abstract: Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: towards a unifying description of conformational transitions, oligomerization and membrane damage
Paper

Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study

The addition of heparin or a point mutation in the segment PHF6* of tau shifts the equilibrium toward more amylogenic conformations.

Graphical abstract: Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study
Paper

Role of aromatic residues in amyloid fibril formation of human calcitonin by solid-state 13C NMR and molecular dynamics simulation

Stable fibril structures of hCT in the antiparallel β-sheet were determined by NMR and MD simulation.

Graphical abstract: Role of aromatic residues in amyloid fibril formation of human calcitonin by solid-state 13C NMR and molecular dynamics simulation
Paper

Cosolvent effects on the fibrillation reaction of human IAPP

Compatible solutes (TMAO) and chaotropic agents (urea) exert different effects on the nucleation and growth process of the fibrils forming islet amyloid polypeptide (IAPP).

Graphical abstract: Cosolvent effects on the fibrillation reaction of human IAPP
Paper

Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20–29) fragments

A key factor in the development of type II diabetes is the loss of insulin-producing beta-cells.

Graphical abstract: Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20–29) fragments
Paper

Effects of membrane interaction and aggregation of amyloid β-peptide on lipid mobility and membrane domain structure

The uptake of GM1 into Aβ aggregates and the attendant membrane damage were microscopically observed.

Graphical abstract: Effects of membrane interaction and aggregation of amyloid β-peptide on lipid mobility and membrane domain structure
Paper

Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers

Molecular dynamics simulations reveal the differences in orientation, adsorption, surface interaction, and selective ion binding between Aβ–POPC and Aβ–POPC–POPG systems.

Graphical abstract: Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers
13 items

About this collection

A collection of articles on the theme of protein misfolding and amyloid diseases from a biophysical viewpoint, guest edited by Ayyalusamy Ramamoorthy (University of Michigan).

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