Abstract：
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.
摘要：
N-烷基化甘氨酸残基是在生物医学和材料科学中使用的拟肽和拟肽-肽杂化物的主要成分。虽然骨架N-烷基化对肽构象的影响已被广泛研究，关于N-胺化对甘氨酸二级结构倾向的影响知之甚少。这里,我们描述了在固体支持物上将N-氨基甘氨酸掺入宿主肽中的方便方案。酰胺对酰肼的取代还提供了用于进一步衍生主链的亲核处理。为了证明后期酰肼改性的实用性，我们合成并评估了含有N-氨基甘氨酸衍生物的聚脯氨酸II螺旋和β-发夹模型系统的稳定性。所描述的程序提供了容易进入肽模拟物库的构象扫描。
