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• W2324102751 abstract "Peptoids (N-substituted glycine oligomers) are widely used peptidomimetics, and an enhanced understanding of their structures is needed to expand their utility, particularly in aqueous applications. We report the synthesis and structural study of four water-soluble peptoids that include strongly helix-promoting (S)-N-1-(naphthylethyl)glycine residues. Peptoid structure changes with both peptoid length and solvent composition. Multiple data support the self-association of the longest peptoid studied here, 1, via hydrophobic interactions in aqueous solutions." @default.
• W2324102751 created "2016-06-24" @default.
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• W2324102751 date "2013-09-19" @default.
• W2324102751 modified "2023-10-07" @default.
• W2324102751 title "Self-Association of Water-Soluble Peptoids Comprising (<i>S</i>)-<i>N</i>-1-(Naphthylethyl)glycine Residues" @default.
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• W2324102751 doi "https://doi.org/10.1021/ol4025502" @default.
• W2324102751 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24050710" @default.
• W2324102751 hasPublicationYear "2013" @default.
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