Self-Association of Water-Soluble Peptoids Comprising (S)‑N‑1-(Naphthylethyl)glycine Residues

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 hel...

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Veröffentlicht in:	Organic letters 2013-10, Vol.15 (19), p.5118-5121
Hauptverfasser:	Fuller, Amelia A, Yurash, Brett A, Schaumann, Erik N, Seidl, Frederick J
Format:	Artikel
Sprache:	eng
Schlagworte:	Circular Dichroism Crystallography, X-Ray Glycine - analogs & derivatives Glycine - chemical synthesis Glycine - chemistry Glycine - metabolism Hydrophobic and Hydrophilic Interactions N-substituted Glycines - chemistry Naphthalenes - chemical synthesis Naphthalenes - chemistry Naphthalenes - metabolism Peptoids - chemical synthesis Peptoids - chemistry Peptoids - metabolism Protein Structure, Secondary Solvents - chemistry Stereoisomerism Water - chemistry
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Zusammenfassung:	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.
ISSN:	1523-7060 1523-7052
DOI:	10.1021/ol4025502