Aβ(1-42) tetramer and octamer structures reveal edge conductivity

Molecular dynamics simulations reveal the importance of amyloid-beta oligomer β-sheet edge conformations in membrane permeabilization - ScienceDirect

The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide

Frontiers Binding mechanism of full-length Aβ40 peptide to a mixed lipid bilayer

Transmembrane Structures for Alzheimer's Aβ1−42 Oligomers

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

Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage

Exploring amyloid oligomers with peptide model systems - ScienceDirect

Eduard Puig, Ph.D. - Freelance

Molecular dynamics simulations reveal the importance of amyloid-beta oligomer β-sheet edge conformations in membrane permeabilization - ScienceDirect

The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide aggregation in membrane-mimetic environments. - Abstract - Europe PMC

Why are the root causes of amyloid-associated diseases so misunderstood and treatments so inadequate?

A β-barrel-like tetramer formed by a β-hairpin derived from Aβ - Chemical Science (RSC Publishing) DOI:10.1039/D3SC05185D