期刊
PEPTIDES
卷 45, 期 -, 页码 28-34出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2013.03.026
关键词
Antimicrobial peptide; Scorpion venom; Pandinus imperator; Amphipathic peptide; Vancomycin-resistant Enterococcus; Antibiotic-resistant pathogen
资金
- China National 973 Research Project, Basic Research and Clinical Application of Venom Peptides from Toxic Animals [2010CB529800]
- Fundamental Research Fund for the Central Universities [CUGL100613]
Three novel cysteine-free venom peptides, which were referred to as Pantinin-1, Pantinin-2 and Pantinin-3, respectively, have been identified from the scorpion Pandinus imperator by cDNA cloning strategy. The precursor of each peptide consists of a signal peptide, a mature peptide with no disulfide bridges, and an acidic propeptide with a typical processing signal. Each of the three peptides is an alpha-helical, cationic and amphipathic molecule with 13 or 14 amino acid residues. Their amino acid sequences are homologous to those of some 13-mer antimicrobial peptides isolated from scorpions. Antimicrobial assay showed that all the three peptides possess relatively strong activities against Gram-positive bacteria and a fungus, but have very weak antimicrobial activities against Gram-negative bacteria. Toxicity assay showed that the three peptides exhibit very low or mild hemolytic activities against human red blood cells. It is interesting to see that Pantinin-3 is able to potently inhibit the growth of vancomycin-resistant Enterococcus (VRE) S13, a pathogen that can cause a number of human infections; this suggests that Pantinin-3 has great potential to be applied in the treatment of VRE infections. Our findings gain new insights into the structure/function relationships of the small linear cationic antimicrobial peptides from scorpions, and provide new templates for designing of antimicrobial agents targeting antibiotic-resistant pathogenic bacteria. (c) 2013 Elsevier Inc. All rights reserved.
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