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

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Dexter, A.F., Fletcher, N.L., Creasey, R.G., Filardo, F. F., Boehm, M.W. and Jack, K.S. (2017) Fabrication and characterization of hydrogels formed from designer coiled-coil fibril-forming peptides. RSC Advances, 7 (44). pp. 27260-27271.

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Article Link: http://dx.doi.org/10.1039/C7RA02811C


AbstractHydrogels 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.

Item Type:Article
Business groups:Horticulture and Forestry Science
Subjects:Science > Microbiology
Agriculture > Agriculture (General) > Agricultural chemistry. Agricultural chemicals
Live Archive:01 Aug 2017 04:16
Last Modified:23 Nov 2022 23:32

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