Per-Residue Program of Multiple Backbone Dihedral Angles of β-Peptoids via Backbone Substitutions
Per-Residue Program of Multiple Backbone Dihedral Angles of β-Peptoids via Backbone Substitutions
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DOI：
10.1021/jacs.9b10496
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发表时间：
2020-02-05
影响因子：
15
通讯作者：
Sando, Shinsuke
中科院分区：
文献类型：
--
作者：
Morimoto, Jumpei;Kim, Jungyeon;Sando, Shinsuke
天然和人工合成寡聚物独特的折叠结构是其独特功能的最基本基础。N-取代的β-肽或β-类肽是合成的低聚物，由于在具有高度模块化合成可及性的单体中存在四个可旋转键，因此具有折叠成多种三维结构的巨大潜力。然而，四个可旋转键的存在对f-类肽的构象控制提出了挑战。在这里，我们报告的每残基编程β两个二面角的β-类肽，这是有用的限制低聚物的构象空间的策略。低聚物被发现形成一个独特的环构象，是稳定的骨架旋转限制。圆二色性和NMR光谱分析和X-射线晶体学分析的低聚物。该策略将显著促进发现β-类肽的许多更独特的折叠结构。
Unique folded structures of natural and synthetic oligomers are the most fundamental basis for their unique functions. N-Substituted beta-peptides, or beta-peptoids, are synthetic oligomers with great potential to fold into diverse three-dimensional structures because of the existence of four rotatable bonds in a monomer with highly modular synthetic accessibility. However, the existence of the four rotatable bonds poses a challenge for conformational control of fi-peptoids. Here, we report a strategy for per-residue programming beta two dihedral angles of beta-peptoids, which is useful for restricting the conformational space of the oligomers. The oligomer was found to form a unique loop conformation that is stabilized by the backbone rotational restrictions. Circular dichroism and NMR spectroscopic analyses and X-ray crystallographic analysis of the oligomer are presented. The strategy would significantly facilitate the discovery of many more unique folded structures of beta-peptoids.