Functional optimisation and mechanistic studies of helical antimicrobial peptides from the skin secretion of the frog, Phyllomedusa tarsius

Moreover, SS1 exhibited anti-proliferative activity against several cancer cell lines. A natural peptide from the dermatoxin family was likewise discovered in the skin secretion of Phyllomedusa tarsius, and named dermatoxin-TA1 (DRT-T1, accession number: P84928). DRT-T1 possessed a broad-spectrum antibacterial activity against lung, breast and brain cancer cell lines.

The results illustrated that the N-terminal of this peptide sequence provided antibacterial and antifungal efficacies using the membrane-damaging mechanism, and the modification of incorporating a positively charged arginine residue at position 11, significantly improved the anti-planktonic activity and salt sensitivity. Overall, this study indicated the rational design and modification of an N-terminal active fragment is ideal for optimizing the dual activities of dermatoxin peptides and it is proposed that N16-11R could be a promising agent for further pharmaceutical research.<br><br><i>Thesis is embargoed until 31 July 2029.</i>