Journal of Pharmaceutical Care & Health Systems
Open Access
ISSN: 2376-0419
+44 1300 500008
ISSN: 2376-0419
+44 1300 500008
Varuna P Panicker and Sisilamma George
Kerala Veterinary and Animal Sciences University, India
Posters & Accepted Abstracts: J Pharma Care Health Sys
Cathelicidin antimicrobial peptides BuMAP-28 and (BuMAP-28)18 were synthesized and used for the present study. Amino acid sequences of the antimicrobial domain were deduced from the gene sequence of myeloid antimicrobial peptide of buffalo. Peptides are highly cationic, amphipathic showed a net charge of +11 for both BuMAP-28 and its analogue; a predicted hydrophobic ratio of 39% for BuMAP-28 and 33% for (BuMAP-28)18. Ramachandran plot analysis indicating a high structural stability for the peptides. In silico structural analysis of the peptides revealed a helix-turn helix which is later confirmed by CD analysis. Biological activity testing of the peptides revealed that the peptide has got a broad spectrum antimicrobial and anti-cancerous activity. Peptides showed wide spectrum of activity against Gram-positive, Gram-negative bacteria, fungi, spirochetes and virus. Peptides are active against even methicillin resistant S. aureus with lower MIC values. In vitro antibacterial and antifungal activities were later confirmed by morphological testing and SEM. Peptides are also proved to be effective against HeLa cell lines. Cytotoxic studies revealed that the truncation of BuMAP-28 could reduce the hemolytic activity when compared to the parent peptide. Murine models injected with Duck Pasteurella (DP1), when treated with the peptides protected 100% of the animals at 12.5 �¼M doses. Studies revealed that the truncation of the peptide could reduce the hemolytic activity without a considerable change in antimicrobial activity.