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• W2894873242 abstract "As proteolytically stable peptidomimetics, peptoids could serve as antifungal agents to supplement a therapeutic field wrought with toxicity issues. We report the improvement of an antifungal peptoid, AEC5, through an iterative structure-activity relationship study. A sarcosine scan was used to first identify the most pharmacophorically important peptoid building blocks of AEC5, followed by sequential optimization of each building block. The optimized antifungal peptoid from this study, β-5, has improved potency towards Cryptococcus neoformans and decreased toxicity towards mammalian cells. For example, the selectivity ratio for C. neoformans over mammalian fibroblasts was improved from 8 for AEC5 to 37 for β-5." @default.
• W2894873242 created "2018-10-12" @default.
• W2894873242 creator A5012956545 @default.
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• W2894873242 date "2018-12-01" @default.
• W2894873242 modified "2023-10-12" @default.
• W2894873242 title "Improved potency and reduced toxicity of the antifungal peptoid AEC5 through submonomer modification" @default.
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• W2894873242 doi "https://doi.org/10.1016/j.bmcl.2018.10.001" @default.
• W2894873242 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6246776" @default.
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