Kasstasin: A novel potent vasoconstrictor peptide from the skin secretion of the African red-legged running frog, Kassina maculata

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• 作者：Xiaohe Li^a ; ^b ; Wanyu Feng^b ; Mei Zhou^a ; Chengbang Ma^a ; Tianbao Chen^a ; Martin Zeller^c ; ^d ; Martin Hornshaw^c ; ^d ; Lei Wang^a ; ^e ; ^{l.wang@qub.ac.uk"" rel=""nofollow} ; Chris Shaw^a ; ^{chris.shaw@qub.ac.uk"" rel=""nofollow}
• 关键词：Amphibian ; Mass spectrometry ; Skin peptides ; Molecular cloning ; Vasoactive
• 刊名：Biochimie
• 出版年：2011
• 出版时间：September 2011
• 年：2011
• 卷：93
• 期：9
• 页码：1537-1542
• 全文大小：711 K

文摘

Amphibian skin secretions are established sources of bioactive peptides. Here we describe the isolation, structural and pharmacological characterisation of a novel vasoconstrictor peptide from the skin secretion of the African hyperoliid frog, Kassina maculata, which exhibits no structural similarity to any known class of amphibian skin peptide. The peptide consists of 21 amino acid residues, FIKELLPHLSGIIDSVANAIK, and is C-terminally amidated. The provisional structure was obtained by MS/MS fragmentation using an Orbitrap mass spectrometer and L/I ambiguities were resolved following molecular cloning of biosynthetic precursor-encoding cDNA. A synthetic replicate of the peptide was found to possess weak antimicrobial and haemolytic activities but was exceptionally effective in constricting the smooth muscle of rat tail artery (EC₅₀ of 25pM). In reflection of its exceptional potency in constricting rat arterial smooth muscle, the peptide was named kasstasin, a derivation of Kassina and “stasis” (stoppage of flow). These data illustrate the continuing potential of amphibian skin secretions to provide novel natural peptide templates for biological evaluation.