Cytotoxic and anticoagulant peptide from Scolopendra subspinipes mutilans venom
Author(s) -
Yi Kong
Publication year - 2013
Publication title -
african journal of pharmacy and pharmacology
Language(s) - English
Resource type - Journals
ISSN - 1996-0816
DOI - 10.5897/ajpp2013.3765
Subject(s) - chemistry , peptide , edman degradation , venom , chromatography , cytotoxicity , biochemistry , peptide sequence , in vitro , gene
Scolopendra subspinipes mutilans venom is a complex mixture of peptides and proteins with many biochemical and pharmacological activities. In this study, a novel peptide was identified by ultra filtration and reverse-phase high performance liquid chromatography (RP-HPLC). The amino acid sequence was FTGGDESRIQEG determined by Edman degradation. The molecular mass was 1296.05 Da determined by electrospray ionisation mass spectrometry (ESI-MS). The novel peptide displayed specific inhibitory effects on the proliferation of human liver cancer (HepG2) and human gastric cancer cells (MGC). It also showed antibacterial activity against the tested bacteria Clostridium perfringens, Staphylococcus epidermidis, and Escherichia coli. Moreover, this peptide prolonged the whole blood clotting time in vivo. This peptide is the first peptide showing cytotoxic and anticoagulant activities identified from S. subspinipes mutilans venom.
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