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Issue 26, 2011
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Formation of α-helix-based twisted ribbon-like fibrils from ionic-complementary peptides

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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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Publication details

The article was received on 08 Apr 2011, accepted on 26 Apr 2011 and first published on 18 May 2011


Article type: Communication
DOI: 10.1039/C1CC12001H
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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