Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 19, Issue 12, Pages 737-744Publisher
WILEY-BLACKWELL
DOI: 10.1002/psc.2569
Keywords
self-assembly; hydrogel; peptide amphiphile; pH sensitive; calcium response
Funding
- National Basic Research Program of China (973 program) [2013CB910700]
- National Natural Science Foundation of China [20932003, 21002007, 21372026]
- Beijing NOVA Program [xx2013010]
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Peptide-based hydrogels have gained much interest for biomedical applications as a result of their biocompatibility. Herein, we reported a synthetic pH-sensitive and calcium-responsive peptide-amphiphilic hydrogel. The sequences of the peptide amphiphiles were derived from the repeat-in-toxin (RTX) motif. At a certain peptide-amphiphile concentration, self-assembly was accompanied by the formation of a rigid, viscoelastic hydrogel at low pH or the presence of calcium ions. Circular dichroism spectra showed that the peptide amphiphiles adopted beta-sheet structure. Meanwhile, as revealed by transmission electron microscopy, the peptide-amphiphile self-assembly was accompanied by the formation of long interconnected nanofibrillar superstructure. Material properties of the resulting peptide-amphiphile hydrogel were characterized using oscillatory sheer rheology, and the storage modulus (G) was found to be one order of magnitude higher than the loss modulus (G), indicating a moderately rigid viscoelastic material. Furthermore, with systematical residue substitution, it was found that the aspartic acid within the repeat-in-toxin sequence of peptide amphiphiles was responsible for the pH and calcium selectivity. The environmental responsiveness, secondary structure, morphology, and mechanical nature of the peptide-amphiphile hydrogel make it a possible material candidate for biomedical and engineering application. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.
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