AbstractThe skin secretions of amphibians attract much attention due to the rich biologically active compounds contained in them. Many peptides from the skin secretions of amphibians have been found to have antimicrobial and enzyme inhibitory effects. In order to identify a new peptide from the skin secretion of the frog, Hylarana nigrovittata, and test its functions, several experiments had been done. In this study, a novel peptide QUB-1704 was isolated from the skin secretion of Hylarana nigrovittata using molecular cloning. After that, the secondary structure of the peptide was predicted online, which turns out that the coils were presented in this peptide. QUB-1704 was synthesized by automated solid phase peptide synthesis and then subjected to MALDI-TOF analysis. Reverse-phase HPLC was used to purify the peptide. QUB-1704 showed no antimicrobial activity against three micro-organism models (E.coli, S.aureus, and C.albicans). Moreover QUB-1704 showed no haemolytic activity against horse blood cells. It showed anticancer activity against H23 cell line at the concentration of 10-4 M. In addition, QUB-1704 showed trypsin inhibitory activity and the Ki was calculated as 3.271 ± 1.362 µM. Further research of this peptide is essential in order to ascertain any other biochemical and pharmacological activities.
Thesis embargoed until 31st October 2024
|Date of Award||Dec 2019|
|Supervisor||Tianbao Chen (Supervisor), Mei Zhou (Supervisor), Lei Wang (Supervisor) & Xinping Xi (Supervisor)|