Document Type
Article
Publication Date
1-30-2024
Publisher
Georg Thieme Verlag KG
Abstract
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.
Recommended Citation
Javed, J. M., Scukas, K., Nguyen, M. T., & Fuller, A. A. (2025). Aromatic Residue Positioning Influences Helical Peptoid Structure in Aqueous Solution. Synlett, 36(6), 724–728. https://doi.org/10.1055/a-2238-5394
Comments
© 2024. The Author(s). This is an open access article published by Thieme under the terms of the Creative Commons Attribution License, permitting copying and reproduction so long as the original work is given appropriate credit. Contents may not be used for commercial purposes or adapted, remixed, transformed or built upon. (https://creativecommons.org/licenses/by/4.0/)