Biophysical Characterization of Chemically Synthesized Antimicrobial Peptide ‘Mastoparan’ and Evaluation of its Activity on Staphylococcus aureus Isolated from Mastitic Milk

Abstract

Antimicrobial peptides (AMPs) are naturally occurring, relatively short (12 to 100 amino acids), positively charged (net charge of +2 to +9), amphiphilic peptide molecules. Antimicrobial peptides are a promising candidate for treatment of diseases caused by pathogenic microbes viz. bacteria, fungi, and viruses (Boman et al., 1995). The key mechanism of action of AMPs is disruption of bacterial membrane by adopting some cationic and amphipathic structure. This membrane acting mechanism involves physicochemical interaction between the peptide and bacterial membrane, formation of peptide quaternary structure and insertion into bacterial membrane and formation of transmembrane pores which ultimately results in membrane permeabilization. AMPs have been isolated from almost all forms of life, including singlecelled microorganisms, insects and other International Journal of Current Microbiology and Applied Sciences ISSN: 2319-7706 Volume 8 Number 11 (2019) Journal homepage: http://www.ijcmas.com