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• W2056169907 abstract "We introduce a novel class of membrane active peptidomimetics, the amphiphilic cationic β3R3-peptides, and evaluate their potential as antimicrobial agents. The design criteria, the building block and oligomer synthesis as well as a detailed structure–activity relationship (SAR) study are reported. Specifically, infrared reflection absorption spectroscopy (IRRAS) was employed to investigate structural features of amphiphilic cationic β3R3-peptide sequences at the hydrophobic/hydrophilic air/liquid interface. Furthermore, Langmuir monolayers of anionic and zwitterionic phospholipids have been used to model the interactions of amphiphilic cationic β3R3-peptides with prokaryotic and eukaryotic cellular membranes in order to predict their membrane selectivity and elucidate their mechanism of action. Lastly, antimicrobial activity was tested against Gram-positive M. luteus and S. aureus as well as against Gram-negative E. coli and P. aeruginosa bacteria along with testing hemolytic activity and cytotoxicity. We found that amphiphilic cationic β3R3-peptide sequences combine high and selective antimicrobial activity with exceptionally low cytotoxicity in comparison to values reported in the literature. Overall, this study provides further insights into the SAR of antimicrobial peptides and peptidomimetics and indicates that amphiphilic cationic β3R3-peptides are strong candidates for further development as antimicrobial agents with high therapeutic index." @default.
• W2056169907 created "2016-06-24" @default.
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• W2056169907 date "2014-04-15" @default.
• W2056169907 modified "2023-10-01" @default.
• W2056169907 title "Amphiphilic Cationic β^3R3-Peptides: Membrane Active Peptidomimetics and Their Potential as Antimicrobial Agents" @default.
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• W2056169907 doi "https://doi.org/10.1021/bm500101w" @default.
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