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- Title
N‐Terminal Charged Residues of Amyloid‐β Peptide Modulate Amyloidogenesis and Interaction with Lipid Membrane.
- Authors
Morris, Clifford; Cupples, Shirin; Kent, Thomas W.; Elbassal, Esmail A.; Wojcikiewicz, Ewa P.; Yi, Peng; Du, Deguo
- Abstract
Abstract: Interactions of amyloid‐β (Aβ) peptides and cellular membranes are proposed to be closely related with Aβ neurotoxicity in Alzheimer's disease. In this study, we systematically investigated the effect of the N‐terminal hydrophilic region of Aβ40 on its amyloidogenesis and interaction with supported phospholipid bilayer. Our results show that modulation of the charge properties of the dynamic N‐terminal region dramatically influences the aggregation properties of Aβ. Furthermore, our results demonstrate that the N‐terminal charged residues play a crucial role in driving the early adsorption and latter remobilization of the peptide on membrane bilayer, and mediating the rigidity and viscoelasticity properties of the bound Aβ40 at the membrane interface. The results provide new mechanistic insight into the early Aβ‐membrane interactions and binding, which may be critical for elucidating membrane‐mediated Aβ amyloidogenesis in a physiological environment and unravelling the origin of Aβ neurotoxicity.
- Subjects
BILAYER lipid membranes; AMYLOID; ALZHEIMER'S disease; PHOSPHOLIPIDS; NEUROTOXICOLOGY; PEPTIDES
- Publication
Chemistry - A European Journal, 2018, Vol 24, Issue 38, p9494
- ISSN
0947-6539
- Publication type
Article
- DOI
10.1002/chem.201801805