AbstractGene-coded antimicrobial peptides (AMPs) are a great source of natural antimicrobial agents and good models for the design of new generation antibiotics. In the meantime, a large number of AMPs have been isolated and characterised from different amphibian species due to their special skin structure and strong adaptability to most types of environment with complex microorganisms.
In this thesis, a novel peptide named QUB-1036 was identified from the lyophilised skin secretion of the European edible frog, Pelophylax kl. esculentus, by both a ‘shotgun’ cloning genomic study and a peptidomic study. After chemical synthesis, QUB-1036 was subjected to bioactivity tests. As a result, QUB-1036 was observed to have no inhibition against microbial growth and was completely devoid of haemolytic activity. It is noteworthy that the novel peptide, QUB-1036, was found to be a bradykinin receptor agonist on rat bladder and uterus. This is one of the few reports of bioactive peptides from the temporin family which have stimulating effects on rat smooth muscles and further studies should focus on its mechanism of action.
|Date of Award||2017|
|Supervisor||Tianbao Chen (Supervisor), Mei Zhou (Supervisor), Lei Wang (Supervisor) & Lei Li (Supervisor)|