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Hp1404, a new antimicrobial peptide from the scorpion Heterometrus petersii.

PloS one (2014-05-16)
Zhongjie Li, Xiaobo Xu, Lanxia Meng, Qian Zhang, Luyang Cao, Wenxin Li, Yingliang Wu, Zhijian Cao
RÉSUMÉ

Antimicrobial peptides have attracted much interest as a novel class of antibiotics against a variety of microbes including antibiotics resistant strains. In this study, a new cationic antimicrobial peptide Hp1404 was identified from the scorpion Heterometrus petersii, which is an amphipathic α-helical peptide and has a specific inhibitory activity against gram-positive bacteria including methicillin-resistant Staphylococcus aureus. Hp1404 can penetrate the membrane of S. aureus at low concentration, and disrupts the cellular membrane directly at super high concentration. S. aureus does not develop drug resistance after multiple treatments with Hp1404 at sub MIC concentration, which is possibly associated with the antibacterial mechanism of the peptide. In addition, Hp1404 has low toxicity to both mammalian cells (HC₅₀  =  226.6 µg/mL and CC₅₀ > 100 µg/mL) and balb-c mice (Non-toxicity at 80 mg/Kg by intraperitoneal injection and LD₅₀  =  89.8 mg/Kg by intravenous injection). Interestingly, Hp1404 can improve the survival rate of the MRSA infected balb-c mice in the peritonitis model. Taken together, Hp1404 may have potential applications as an antibacterial agent.

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Sigma-Aldrich
Lipopolysaccharides from Escherichia coli O111:B4, purified by gel-filtration chromatography
Sigma-Aldrich
Acide lipotéichoïque from Staphylococcus aureus, bacterial cell wall polymer