Aromatic residue positioning influences helical peptoid structure in aqueous solution

Synlett Pub Date : 2024-01-04 DOI:10.1055/a-2238-5394
Jwwad M. Javed, Katherine Scukas, Michelle T. Nguyen, Amelia Fuller
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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.

Abstract Image

芳香族残基定位影响水溶液中的螺旋蛋白胨结构
水溶性拟肽物,包括类蛋白胨,是具有生物相关性的两亲性螺旋肽的有前途的功能替代物。我们设计、制备并使用圆二色性(CD)光谱研究了 20 种具有预测螺旋结构的两亲拟肽六聚物。评估了水溶液中芳香族残基和带电残基对蛋白胨六聚体螺旋结构的特定位点贡献,结果表明芳香族残基的位置对结构的影响最大。
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