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

Bera, S., Arad, E., Schnaider, L., Shaham-Niv, S., Castelletto, V., Peretz, Y., Zaguri, D., Jelinek, R., Gazit, E. and Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 (2019) Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core. Chemical Communications, 55 (59). pp. 8595-8598. ISSN 1359-7345 doi: 10.1039/C9CC03654G

Abstract/Summary

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.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/85148
Identification Number/DOI	10.1039/C9CC03654G
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	Royal Society of Chemistry
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