Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation. Issue 5 (10th November 2015)

• Record Type: Journal Article
• Authors: Korshavn, Kyle J.; Bhunia, Anirban; Lim, Mi Hee; Ramamoorthy, Ayyalusamy
• Is Part Of: Chemical communications. Volume 52:Issue 5(2016)
• Page Start: 882
• Page End: 885
• Publication Date: 2015-11-10
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c5cc08634e
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-β (Aβ) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. Abstract : Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-β (Aβ) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. We have identified a conserved binding mode of Aβ40 on lipid bilayer surfaces with a conserved helix containing the self-recognition site (K16-E22).