Alzheimer's disease: which type of amyloid-preventing drug agents to employ?
The amyloid hypothesis and toxic ion channel formation in Alzheimer's disease.
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.
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.
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.
Stereochemical effects on the aggregation and biological properties of the fibril-forming peptide [KIGAKI]3 in membranes
Conformational equilibria of [KIGAKI]3.
Amyloid-β–neuropeptide interactions assessed by ion mobility-mass spectrometry
Small neuropeptides can bind to amyloid-β and modulate their aggregation in vitro.
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.
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.
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.
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).
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.
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.
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.
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).