Senegalin: a novel antimicrobial/myotropic hexadecapeptide from the skin secretion of the African running frog, Kassina senegalensis

Hui Wang, Renjie Li, Xinping Xi, Teng Meng, Mei Zhou, Lei Wang, Yingqi Zhang, Tianbao Chen, Christopher Shaw

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

Amphibian skin is a rich and unique source of novel bioactive peptides most of which are endowed with either antimicrobial or pharmacological properties. Here we report the identification and structural characterization of a novel peptide, named senegalin, which possesses both activities. Senegalin is a hexadecapeptide amide (FLPFLIPALTSLISSL-NH2) of unique primary structure found in the skin secretion of the African running frog, Kassina senegalensis. The structure of the biosynthetic precursor of senegalin, deduced from cloned skin cDNA, consists of 76 amino acid residues and displays the typical domain organization of an amphibian skin peptide precursor. Both natural senegalin and its synthetic replicate displayed antimicrobial and myotropic activities. Senegalin was active against Staphylococcus aureus (MIC 50µM) and Candida albicans (MIC 150µM) but was nonhaemolytic at concentrations up to and including 150µM. In contrast, senegalin induced a dose-dependent contraction of rat urinary bladder smooth muscle (EC50 2.9nM) and a dosedependent relaxation of rat tail artery smooth muscle (EC50 37.7nM). Senegalin thus represents a prototype biologically-active amphibian skin peptide and illustrates the fact thatamphibian skin secretion peptidomes continue to be unique sources of such molecules.
Original languageEnglish
Pages (from-to)1347-1355
JournalAmino Acids
Volume44
Issue number5
Early online date22 Feb 2013
DOIs
Publication statusPublished - May 2013

Keywords

  • Amphibian; Peptide; Antimicrobial; Smooth Muscle; Molecular Cloning

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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