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Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation.

Chem. Commun. (Camb.). 2016; 
KorshavnKyle J,BhuniaAnirban,LimMi Hee,RamamoorthyAyyalu
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Recombinant Proteins Unlabeled Ab40 (> 95% purity) was purchased from Genscript (Piscataway, NJ, USA). Get A Quote

摘要

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).

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