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Issue 44, 2017
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Fabrication and characterization of hydrogels formed from designer coiled-coil fibril-forming peptides

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Abstract

Hydrogels are soft solids that represent attractive matrices for tissue engineering, wound healing and drug delivery. We previously reported an α-helical peptide, AFD19, that forms fibrils and hydrogels at pH 6, but precipitates under physiological conditions. We now show that a single targeted change in AFD19 yields peptide AFD36, which gels at physiological pH and in the presence of salt. Furthermore, we present a simple method for homogeneous sol–gel conversion through pH titration with sodium bicarbonate followed by loss of carbon dioxide. Chemical and thermal denaturation studies show AFD36 self-assembles to give stable α-helical structures, forming fibrils of 3.8–3.9 nm diameter at pH 4.0–7.0 as shown by small-angle X-ray scattering and atomic force microscopy. An AFD36 gel at 0.35% (w/v) showed an elastic modulus of 350 Pa. Mouse fibroblasts exhibited low cellular toxicity and spread morphologies when grown on the gel as a preliminary proof of principle towards cell culture studies. These peptide gels offer a molecularly simple, biodegradable alternative to polymer-based systems for biomedical applications.

Graphical abstract: Fabrication and characterization of hydrogels formed from designer coiled-coil fibril-forming peptides

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Publication details

The article was received on 08 Mar 2017, accepted on 10 May 2017 and first published on 23 May 2017


Article type: Paper
DOI: 10.1039/C7RA02811C
Citation: RSC Adv., 2017,7, 27260-27271
  • Open access: Creative Commons BY-NC license
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    Fabrication and characterization of hydrogels formed from designer coiled-coil fibril-forming peptides

    A. F. Dexter, N. L. Fletcher, R. G. Creasey, F. Filardo, M. W. Boehm and K. S. Jack, RSC Adv., 2017, 7, 27260
    DOI: 10.1039/C7RA02811C

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