Discovery and evaluation of trypsin inhibitor peptides and analogues from Schmacker’s frog, Odorrana schmackeri

These peptides can trigger different physiological responses due to their remarkable specificity and affinity to cell surface receptors. The various biological and pharmaceutical functions of peptides present a wealth of opportunities, rendering them as promising candidates for therapeutic development.

In this research, a novel peptide belonging to the Bowman-Birk type inhibitor (BBI) family, was isolated and identified from the skin secretion of the frog, Odorrana schmackeri. The biofunctionality was studied and several analogues were generated by rational structural modifications to the parent peptide for optimizing the antimicrobial or anticancer activities. Then, several strategies were used to modify a second type of trypsin inhibitor peptide to validate the rationale and effectiveness of the structural modification strategies.