Peptides derived from frog skin secretion have great potential as drug leads as they exhibit many bioactive functions. In this study, the precursor peptide of Lividin-AW was identified from the skin secretion of the Chinese torrent frog (Amolops wuyiensis) by using ‘shotgun’ cloning and its encoded mature peptide, sequenced as AVPLIYNRPGVYVTKRPK-NH2, was synthesised by Fmoc-solid phase peptide synthesis. The structure of the synthetic peptide was confirmed by matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometry and purified by reversed-phase high performance liquid chromatography (RP-HPLC). To determine the bioactive function of Lividin-AW, a series of bioactivity assays, including antimicrobial assays, cell viability assays, a trypsin inhibition assay and a haemolysis assay, were conducted and the results showed that Lividin-AW exhibited weak antimicrobial activity against Candida albicans (MIC=128µM), Staphylococcus aureus (MIC=512 µM) and Escherichia coli (MIC=512 µM), with negligible haemolytic activity, but neither trypsin inhibition activity nor anticancer activity were detected.
|Date of Award||25 Aug 2017|
- Queen's University Belfast
|Supervisor||Christopher Shaw (Supervisor), Tianbao Chen (Supervisor), Mei Zhou (Supervisor), Lei Wang (Supervisor), Xinping Xi (Supervisor) & Chengbang Ma (Supervisor)|