pH and secondary structure instructed aggregation to a thixotropic hydrogel by a peptide amphiphile

Peptide-amphiphile (PA)-based supramolecular thixotropic hydrogels are useful in medical sciences due to multiple advantageous features along with its biocompatibility and biodegradability. In this work, we have developed a self-assembled peptide-based hydrogel from a β -sheet forming short PA. Hydrogelation of the PA is controlled by pH and consequent changes in secondary structures attained by the PA. Under acidic conditions, the PA remains in random coil conformation. While increasing the pH to 9, a rapid transformation to anti-parallel β -sheet leads to a strong hydrogel. Interestingly, the disulphide-linked dimer of the PA failed to attain such aggregation pattern. The pH-induced sol–gel–sol transition can be achieved for several cycles without any change in aggregation pattern. The hydrogel was also found to show thixotropic rheological behaviour and thus, it can be utilized as an injectable hydrogel for biomedical applications.