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

Abstract : 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 a strategy that can lead to the discovery of novel small CAMPs with greatly enhanced antimicrobial activity and retained antibiofilm potential. We geared our efforts towards i) the N-terminal cysteine functionalization of a previously reported small synthetic cationic peptide (peptide 1037, KRFRIRVRV-NH2), ii) its dimerization through a disulfide bond, and iii) a preliminary antimicrobial activity assessment of the newly prepared dimer against Pseudomonas aeruginosa and Burkholderia cenocepacia, pathogens responsible for the formation of biofilms in lungs of individuals with cystic fibrosis. This dimer is of high interest as it does not only show greatly enhanced bacterial growth inhibition properties compared to its pep1037 precursor (up to 60 times), but importantly, also displays antibiofilm potential at sub-MICs. Our results suggest that the reported dimer holds promise for its use in future adjunctive therapy, in combination with clinically-relevant antibiotics.
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Amal Thamri, Myriam Létourneau, Alex Djoboulian, David Chatenet, Eric Déziel, et al.. Peptide modification results in the formation of a dimer with a 60-fold enhanced antimicrobial activity.. PLoS ONE, Public Library of Science, 2017, 12 (3), pp.e0173783. ⟨10.1371/journal.pone.0173783⟩. ⟨pasteur-01533721⟩

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