Issue 58, 2013
From the journal:

Chemical Communications

Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils†

Yoav Raz,ab   Boris Rubinov,ab   Maayan Matmor,bc   Hanna Rapaport,bd   Gonen Ashkenasy*ab  and  Yifat Miller*ab  

* Corresponding authors

a Department of Chemistry, Ben-Gurion University of the Negev, Beér-Sheva 84105, Israel
E-mail: ymiller@bgu.ac.il, gonenash@bgu.ac.il

b The Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beér-Sheva 84105, Israel

c Department of Materials Engineering, Ben-Gurion University of the Negev, Beér-Sheva 84105, Israel

d Department of Biotechnology Engineering, Ben-Gurion University of the Negev, Beér-Sheva 84105, Israel

Abstract

The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.

Graphical abstract: Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils

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Article information

DOI
https://doi.org/10.1039/C3CC42879F
Article type
Communication
Submitted
18 Apr 2013
Accepted
30 May 2013
First published
30 May 2013

Chem. Commun., 2013,49, 6561-6563

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Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils

Y. Raz, B. Rubinov, M. Matmor, H. Rapaport, G. Ashkenasy and Y. Miller, Chem. Commun., 2013, 49, 6561 DOI: 10.1039/C3CC42879F

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