Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch.
The scorpion venom peptides with no disulfide bridge are rarely identified and poorly characterized so far. Here, we report the identification and characterization of four novel disulfide-bridge-free venom peptides (BmKa1, BmKa2, BmKb1 and BmKn2) from Buthus martensii Kasch. BmKa1 and BmKa2 are very acidic and hydrophilic, showing no any similarity to other proteins, whereas BmKb1 and BmKn2 both are basic, alpha-helical peptide with an amidated C-terminus, showing a little homology with other peptides. Functional tests with synthetic peptide showed that BmKn2 has strong antimicrobial activity against both Gram-positive and Gram-negative bacteria, whereas BmKb1 has weak activity in inhibiting the growth of these bacteria.
Zeng
Xian-Chun
XC
Department of Biotechnology, Institute of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China. zengx@nhlbi.nih.gov
Wang
San-Xia
SX
Zhu
Yan
Y
Zhu
Shun-Yi
SY
Li
Wen-Xin
WX
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D019295:Computational Biology; D004220:Disulfides / Q000737:chemistry*; D015723:Gene Library; D008969:Molecular Sequence Data; D012604:Scorpion Venoms / Q000737:chemistry*; D012605:Scorpions / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D023181:Antimicrobial Cationic Peptides; D004220:Disulfides; D012604:Scorpion Venoms