Aromatic Residue Positioning Influences Helical Peptoid Structure in Aqueous Solution

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Water-soluble peptidomimetics, including peptoids, are promising functional surrogates for biologically relevant, amphiphilic, helical peptides. Twenty amphiphilic peptoid hexamers with predicted helical structures were designed, prepared, and studied using circular dichroism (CD) spectroscopy. The site-specific contributions of aromatic and charged residues to the helical structure of peptoid hexamers in aqueous solution was evaluated, revealing that aromatic residue positioning most significantly impacts structure.

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: Aromatic Residue Positioning Influences Helical Peptoid Structure in Aqueous Solution ; day:30 ; month:01 ; year:2024
Synlett ; (30.01.2024)

Contributor: Javed, Jwwad M.
Scukas, Katherine
Nguyen, Michelle T.
Fuller, Amelia A.

DOI: 10.1055/a-2238-5394

URN: urn:nbn:de:101:1-2024031411200251827977

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:51 AM CEST

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Javed, Jwwad M.
Scukas, Katherine
Nguyen, Michelle T.
Fuller, Amelia A.

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Aromatic Residue Positioning Influences Helical Peptoid Structure in Aqueous Solution

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Other Objects (12)

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