Discovery and functional assessment of short α-helical peptides from the defensive skin secretions of amphibians

QUB-1426 and 6K-1426, with potent antimicrobial and anticancer activities both in vitro and in vivo, were regarded as competitive drug candidates. In Chapter 4, the structure-function characteristics of the peptides were studied. This work described a clear relationship between the peptide function and physiochemical parameters including charge, secondary structure, hydrophobicity and amphipathy. 6K-9A with an ideal charge, hydrophobicity and well-defined α-helical structure, was the most potent candidate peptide found here.

In Chapter 5, the peptide modification study revolved around a known, moderately functional peptide, aurein 1.2. The introduction of known sequences into the peptide proved an efficient option for short peptides and here, the –IIKK- cell-penetrating region-modified analogues demonstrated outstanding anti-cancer activities, and the KLA-modified analogue, KLA-2, was the most potent antimicrobial agent here.<br><br><i>Thesis is embargoed until 31 July 2028</i>.<br><br>