Assessing N- and C-Terminus Amino Acids in the Lytic Activity of Antimicrobial Peptides
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The overuse of antibiotics in the fields of medicine and food production have led to an unprecedented trend of antibiotic resistance that has been called “as big a risk as terrorism”. A potential solution to this dilemma is Antimicrobial Peptides (AMPs). These strands, consisting of 12 to 50 amino acids, are produced in all living organism’s immune systems. This experiment assessed the functionality of the N and C termini of melittin, which is found naturally in bee venom. Functionality was assessed by measuring the capability of test peptides to lyse liposomes, RBCs, E. coli, and S. aureus. The results show that the N and C termini of melittin inhibit the growth of E. coli, and S. aureus, but do not enable lysis of human erythrocytes or DPPC/DPPG liposomes. It was also demonstrated that the N-terminus of the nNOS peptide, an endogenous peptide is important for lysing the gram-positive S. aureus.