Issue 59, 2019

Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

Abstract

The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.

Graphical abstract: Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

Supplementary files

Article information

Article type
Communication
Submitted
12 May 2019
Accepted
02 Jul 2019
First published
02 Jul 2019

Chem. Commun., 2019,55, 8595-8598

Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

S. Bera, E. Arad, L. Schnaider, S. Shaham-Niv, V. Castelletto, Y. Peretz, D. Zaguri, R. Jelinek, E. Gazit and I. W. Hamley, Chem. Commun., 2019, 55, 8595 DOI: 10.1039/C9CC03654G

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