Team:SVCE CHENNAI/CATIONIC AMPs
Antimicrobial peptides are an attractive phase of clinical research. These are preferred because of their selectivity, speed of action and because bacteria don’t easily develop resistance against them. Of particular interest among antimicrobial peptides are the cationic antimicrobial peptides(cAMPs). Several studies have been conducted to explore cAMPs as potential candidates for replacing common antibiotics. A study conducted by Wenzel et al in 2014 showed that peptides having alternating repeats of arginine and tryptophan acted as excellent antimicrobials. But, the peptides with only arginine and tryptophan had a very low half-life. So two peptides were designed, one with glycine and one without.
Studies which were conducted by Wenzel et al on a hexapeptide containing only arginine and tryptophan showed : 1. Their peptide was effective against Gram-positive bacteria including Methicillin Resistant Staphylococcus aureus. 2. It was moderately effective against Gram-negative bacteria. 3. It had low haemolytic activity and very low toxicity towards human cells. 4. Their peptide attacked the bacterial cell membrane by integrating itself into the membrane and causes membrane depolarization.
PEPTIDE SEQUENCE 1:
RWRWRWM-NH2(5’- ATG TGG CGT TGG CGT TGG CGT TAA – 3’)
THE N-END RULE:
According to the N-end Rule, the presence of arginine or tryptophan at the N-end of the peptide would give it a very low half-life. So we introduced a couple of glycine residues in the peptide for increasing its half-life.
PEPTIDE SEQUENCE 2:
RWRWRWGGM-NH2(5’- ATG GGC GGC TGG CGT TGG CGT TGG CGT TAA – 3’)
PLASMID SEQUENCE:
