扁桃体
拟肽
聚脯氨酸螺旋
酰肼
化学
衍生化
肽
组合化学
胺化
烷基化
亲核取代
甘氨酸
立体化学
还原胺化
肽键
固相合成
氨基酸
有机化学
生物化学
高效液相色谱法
催化作用
作者
Syrah K. Starnes,Juan R. Del Valle
出处
期刊:Methods in Enzymology
日期:2024-01-01
卷期号:: 1-26
标识
DOI:10.1016/bs.mie.2024.04.018
摘要
N-alkylated glycine residues are the main constituent of peptoids and peptoid-peptide hybrids that are employed across the biomedical and materials sciences. While the impact of backbone N-alkylation on peptide conformation has been extensively studied, less is known about the effect of N-amination on the secondary structure propensity of glycine. Here, we describe a convenient protocol for the incorporation of N-aminoglycine into host peptides on solid support. Amide-to-hydrazide substitution also affords a nucleophilic handle for further derivatization of the backbone. To demonstrate the utility of late-stage hydrazide modification, we synthesized and evaluated the stability of polyproline II helix and β-hairpin model systems harboring N-aminoglycine derivatives. The described procedures provide facile entry into peptidomimetic libraries for conformational scanning.
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