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

Santu Bera, Elad Arad, Lee Schnaider, Shira Shaham-Niv, Valeria Castelletto, Yossef Peretz, Dor Zaguri, Raz Jelinek, Ehud Gazit, Ian W. Hamley

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish
Pages (from-to)8595-8598
Number of pages4
JournalChemical Communications
Volume55
Issue number59
DOIs
StatePublished - 1 Jan 2019

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