Issue 26, 2011
From the journal:

Chemical Communications

Formation of α-helix-based twisted ribbon-like fibrils from ionic-complementary peptides†

Dawei Zou,a   Yi Cao,a   Meng Qin,*a   Weimin Daia  and  Wei Wang*a  

* Corresponding authors

a National Laboratory of Solid State Microstructure and Department of Physics, Nanjing University, Nanjing 210093, China
E-mail: qinmeng@nju.edu.cn, wangwei@nju.edu.cn

Abstract

Ionic-complementary peptides (ICPs) are well known for their strong propensity to form amyloid-like β-sheet fibrils. Here, we present the first example that α-helical based ICPs can self-assemble into a highly ordered fibrillar structure. Intriguingly, the individual α-helices in such fibrils are arranged shoulder-to-shoulder, making them distinct from conventional coiled-coil-based fibrils.

Graphical abstract: Formation of α-helix-based twisted ribbon-like fibrils from ionic-complementary peptides

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Article information

DOI
https://doi.org/10.1039/C1CC12001H
Article type
Communication
Submitted
08 Apr 2011
Accepted
26 Apr 2011
First published
18 May 2011

Chem. Commun., 2011,47, 7413-7415

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Formation of α-helix-based twisted ribbon-like fibrils from ionic-complementary peptides

D. Zou, Y. Cao, M. Qin, W. Dai and W. Wang, Chem. Commun., 2011, 47, 7413 DOI: 10.1039/C1CC12001H

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