title: Senegalin: a novel antimicrobial/myotropic hexadecapeptide from the skin secretion of the African running frog, Kassina senegalensis.
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 50 μM) and Candida albicans (MIC 150 μM) but was non-haemolytic at concentrations up to and including 150 μM. In contrast, senegalin induced a dose-dependent contraction of rat urinary bladder smooth muscle (EC50 2.9 nM) and a dose-dependent relaxation of rat tail artery smooth muscle (EC50 37.7 nM). Senegalin thus represents a prototype biologically active amphibian skin peptide and illustrates the fact that amphibian skin secretion peptidomes continue to be unique sources of such molecules.
authors: Natural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, 97 Lisburn Road, BT9 7BL Belfast, Northern Ireland, UK.
authors: Hui
authors: H
authors: Wang
authors: Renjie
authors: R
authors: Li
authors: Xinping
authors: X
authors: Xi
authors: Teng
authors: T
authors: Meng
authors: Mei
authors: M
authors: Zhou
authors: Lei
authors: L
authors: Wang
authors: Yingqi
authors: Y
authors: Zhang
authors: Tianbao
authors: T
authors: Chen
authors: Chris
authors: C
authors: Shaw
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D001001:Anura / Q000378:metabolism*; D001483:Base Sequence; D003001:Cloning, Molecular; D066298:In Vitro Techniques; D008297:Male; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D009131:Muscle, Smooth, Vascular / Q000187:drug effects / Q000502:physiology; D017433:Protein Structure, Secondary; D051381:Rats; D017208:Rats, Wistar; D012867:Skin / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000187:drug effects; D001743:Urinary Bladder / Q000187:drug effects / Q000502:physiology; D014665:Vasodilator Agents / Q000737:chemistry / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D014665:Vasodilator Agents