Peptide modification results in the formation of a dimer with a 60-fold enhanced antimicrobial activity

• DOI: 10.1371/journal.pone.0173783
• Publication Date: 2017-03-15T14:24:00Z
• Authors: Amal Thamri; Myriam Létourneau; Alex Djoboulian; David Chatenet; Eric Déziel; Annie Castonguay; Jonathan Perreault
• Keywords: Burkholderia cenocepacia

Cationic antimicrobial peptides (CAMPs) occur naturally in numerous organisms and are considered as a class of antibiotics with promising potential against multi-resistant bacteria. Herein, we report strategy that can lead to the discovery novel small CAMPs greatly enhanced activity retained antibiofilm potential. We geared our efforts towards i) N-terminal cysteine functionalization previously reported synthetic cationic peptide (peptide 1037, KRFRIRVRV-NH2), ii) its dimerization through disulfide bond, iii) preliminary assessment newly prepared dimer Pseudomonas aeruginosa Burkholderia cenocepacia, pathogens responsible for formation biofilms lungs individuals cystic fibrosis. This is high interest it does not only show bacterial growth inhibition properties compared pep1037 precursor (up 60 times), but importantly, also displays at sub-MICs. Our results suggest holds promise use future adjunctive therapy, combination clinically-relevant antibiotics.