Self‐assembly of pH and calcium dual‐responsive peptide‐amphiphilic hydrogel

This is the authors' abstract. We don't add key points for this paper.

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.