N-Terminal Charged Residues of Amyloid-β Peptide Modulate Amyloidogenesis and Interaction with Lipid Membrane.

Autor: Morris C; Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA., Cupples S; Department of Civil, Environmental and Geomatics Engineering, Florida Atlantic University, Boca Raton, FL, 33431, USA.; Department of Ocean and Mechanical Engineering, Florida Atlantic University, Boca Raton, FL, 33431, USA., Kent TW; Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA., Elbassal EA; Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA., Wojcikiewicz EP; Department of Biomedical Science, Florida Atlantic University, Boca Raton, FL, 33431, USA., Yi P; Department of Civil, Environmental and Geomatics Engineering, Florida Atlantic University, Boca Raton, FL, 33431, USA., Du D; Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA.
Jazyk: angličtina
Zdroj: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2018 Jul 05; Vol. 24 (38), pp. 9494-9498. Date of Electronic Publication: 2018 Jun 06.
DOI: 10.1002/chem.201801805
Abstrakt: 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.
(© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Databáze: MEDLINE
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