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

RSC Adv. 2017; 
A. F. Dexter‡ *a,  N. L. Fletcher§ a,  R. G. Creaseyb,  F. Filardo¶ a,  M. W. Boehmb and K. S. Jack
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Peptide Synthesis Reagents were of the highest grade available. Water was purified using an Elga Purelab Classic and had a resistivity of >18.2 MΩ cm. Glassware was acid-cleaned as previously described.39 Peptides AFD19 (Ac-LKELAKV LHELAKL VSEALHA-CONH2, FW 2354) and AFD36 (Ac-LKELAKV LHELAKL VKEALHA-CONH2, FW 2395) were synthesized and purified by GenScript (Piscataway, New Jersey). The final purity was >95% in each case. The peptide content of the solid was determined by quantitative amino acid analysis (Australian Proteome Analysis Facility, Sydney). The charge on each peptide as a function of pH was estimated as described previously.36 Get A Quote

摘要

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 s... More

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