Identification of a Novel Vasodilatory Octapeptide from the Skin Secretion of the African Hyperoliid Frog, Kassina senegalensis

Qiang Du, Hui Wang, Chengbang Ma, Yue Wu, Xinping Xi, Mei Zhou, Tianbao Chen, Chris Shaw, Lei Wang

Research output: Contribution to journalArticle

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Abstract

The defensive skin secretions of amphibians continue to be an excellent source of novel biologically-active peptides. Here we report the identification and pharmacological activity of a novel C-terminally amided myotropic octapeptide from the skin secretion of the African hyperoliid frog, Kassina senegalensis. The 8-amino acid peptide has the following primary structure: WMSLGWSL-amide and has a molecular mass of 978 Da. The primary structure and organisation of the biosynthetic precursor of WL-8 amide was successfully deduced from cloned skin secretion-derived cDNA. The open-reading frame encoded a single copy of WL-8, located at the C-terminus. Synthetic WL-8 amide was found to cause relaxation of rat tail artery smooth muscle with an EC50 of 25.98 nM. This peptide is unique in terms of its primary structure and is unlike any other peptide previously isolated from an amphibian source which has been archived in the NCBI database. WL-8 amide thus represents the prototype of a novel family of myotropic peptide from amphibian defensive skin secretions
Original languageEnglish
Article number1215
Number of pages9
JournalMolecules
Volume22
DOIs
Publication statusPublished - 19 Jul 2017

Keywords

  • amphibian; skin secretion; peptide; smooth muscle

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