Journal
CHEMICAL BIOLOGY & DRUG DESIGN
Volume 90, Issue 6, Pages 1155-1160Publisher
WILEY
DOI: 10.1111/cbdd.13035
Keywords
antimicrobial peptide; MRSA; Omiganan; skin infection; Staphylococcus aureus
Funding
- Agency for Science, Technology and Research
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Staphylococcus aureus is the primary pathogen responsible for the majority of human skin infections, and meticillin-resistant S.aureus (MRSA) currently presents a major clinical concern. The overuse of Mupirocin, the first-line topical antibacterial drug over 30years, has led to the emergence of Mupirocin-resistant MRSA, creating a clinical concern. The antimicrobial peptide Omiganan was touted to be a promising antibacterial drug candidate due to its rapid membrane-disrupting bactericidal mode of action, entering clinical trials in 2005 as a topical gel to prevent catheter site infections. However, drug development ceased in 2009 due to a lack of efficacy. We postulate this to be due to proteolytic degradation caused by endogenous human skin proteases. Herein, we tested our hypothesis using Omiganan and its all-D enantiomer in a human skin protease stability assay, followed by anti-MRSA activity assay against of a panel of clinical MRSA isolates, a bactericidal/static determination and a time-kill assay to gauge all-D Omiganan's potential for further topical antibacterial drug development.
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