AbstractPeptides from amphibian skin secretions are widely studied because of their unique physiological and neurotransmitter roles, and are commonly acknowledged as one of the most indispensable elements during the survival and evolution of amphibians. Among these peptides, bradykinin-related peptides (BRPs) stand out from the considerable number of peptide families due to their close relationship with the regulation of mammalian physiological and pathological processes.
Here, a BRP precursor-encoding transcripts was deduced from cDNA libraries from the skin secretions of the Chinese piebald odorous frog, Odorrana schmackeri, through the application of the molecular cloning method of ‘shotgun’ cloning and sequencing. The mature peptide was subsequently synthesised by solid phase peptide synthesis (SPPS) and its authenticity was confirmed using RP-HPLC and MALDI-TOF mass spectrometry. Later, several biological functions of this novel peptide were investigated.
Results indicated a dose-dependent contractile activity of the peptide on rat bladder smooth muscle, a dose-dependent relaxation on rat arterial smooth muscle and a BK inhibitor function on rat ileum. Besides, increased frequency of contraction was observed on rat uterus smooth muscle following application of this novel peptide. No haemolytic effect was observed on mammalian red blood cells, and no anti-cancer activity or antimicrobial function was found using the bioassays described in this research. Studies on this novel BRP have provided beneficial information and may act as a potential reference for novel drug design.
|Date of Award
|Lei Wang (Supervisor), Tianbao Chen (Supervisor), Christopher Shaw (Supervisor), Mei Zhou (Supervisor), Xinping Xi (Supervisor), Chengbang Ma (Supervisor), Yuxin Wu (Supervisor) & Lei Li (Supervisor)