Antibacterial activity of a peptide derived from HIV-1 MN strain gp41 envelope glycoprotein against methicillin-resistant Staphylococcus aureus

ABSTRACT

Peptides derived from HIV-1 transmembrane proteins have been extensively studied for antimicrobial activities, and they are known as antimicrobial peptides [AMPs]. These AMPs have also been reported to potently combat the drug-resistant microbes. In this study, we demonstrated that peptide no. 6383 originated from HIV-1 MN strain membrane-spanning domain of gp41 was active [2-log reductions] at 100 micro g/mL [56.5 micro M] against methicillin-resistant Staphylococcus aureus [MRSA] in 10% and 50% human plasma-supplemented phosphate buffered saline [PBS]. The activity was further enhanced [3-log reductions] in the presence of 5% human serum albumin [HSA] alone. All bactericidal activities were achieved within 6 hours. At 100 micro g/mL, the peptide showed only 13% toxicity against human erythrocytes. This peptide can serve as an attractive template for a design of a novel peptide antibiotic against drugresistant bacteria. By sequence-specific engineering or modifications, we anticipated that the bactericidal activity and the reduced toxicity against human erythrocytes will be improved