Modifications on amphiphilicity and cationicity of unnatural amino acid containing peptides for the improvement of antimicrobial activity against pathogenic bacteria

Journal of Peptide Science : an Official Publication of the European Peptide Society
Junichi TairaHiroaki Kodama

Abstract

The widespread natural sources-derived cationic peptides have been reported to reveal bacterial killing and/or growth-inhibiting properties. Correspondingly, a number of artificial peptides have been designed to understand antibacterial mechanism of the cationic peptides. These peptides are expected to be an alternative antibiotic against drug-resistant pathogenic bacteria because major antimicrobial mechanism of cationic peptides involves bacterial membrane disorder, although those availabilities have not been well evaluated. In this study, cationic peptides containing Aib were prepared to evaluate the availability as an antimicrobial agent, especially against representative pathogenic bacteria. Among them, BRBA20, consisting of five repeated Aib-Arg-Aib-Ala sequences, showed strong antibacterial activity against both Gram-negative and Gram-positive bacteria, including methicillin-resistant Staphylococcus aureus. Additionally, growth of Serratia marcescens and multidrug-resistant Pseudomonas aeruginosa, known as proteases-secreting pathogenic bacteria, were also completely inhibited by BRBA20 under 20 µg/ml peptide concentrations. Our results suggested availabilities of Aib-derived amphiphilicity and protease resistance in the...Continue Reading

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Citations

Feb 13, 2014·Journal of Peptide Science : an Official Publication of the European Peptide Society·Roksana Wałęsa, Małgorzata A Broda
Dec 20, 2011·Organic & Biomolecular Chemistry·Marta De ZottiClaudio Toniolo
Feb 11, 2021·ChemMedChem·Hidetomo YokooYosuke Demizu
Aug 23, 2019·Chemical Reviews·Johann MoschnerBeate Koksch
Dec 20, 2013·Journal of Medicinal Chemistry·Artem CherkasovAlexander Tropsha

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