Residue-based program of a β-peptoid twisted strand shape via a cyclopentane constraint
Residue-based program of a β-peptoid twisted strand shape via a cyclopentane constraint
复制标题
通过环戊烷约束进行基于残基的 β-类肽扭曲链形状编程
DOI：
10.1039/d2ob01300b
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发表时间：
2022
期刊：
影响因子：
--
通讯作者：
Sando S.
中科院分区：
文献类型：
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作者：
Kim J;Kobayashi H;Yokomine M;Shiratori Y;Ueda T;Takeuchi K;Umezawa K;Kuroda D;Tsumoto K;Morimoto J;Sando S.
N-取代肽，如类肽和β-类肽，已被报道具有独特的结构，具有不同的功能，如催化和操纵生物分子功能。最近，通过限制所有骨架二面角的键旋转的单体形状的预组织已被证明是有用的从头设计的类肽结构。这种设计策略迄今尚未探索用于β-类肽;迄今为止，尚未报道预组装的β-类肽单体。在这里，我们报告了β-类肽的第一个设计策略，其中所有四个骨架二面角（ω，θ，θ，ω）在每个残基的基础上被旋转限制。环戊烷约束的引入实现了预组装的单体结构，并导致具有稳定的扭曲链形状的β-拟肽。
N-Substituted peptides, such as peptoids and β-peptoids, have been reported to have unique structures with diverse functions, like catalysis and manipulation of biomolecular functions. Recently, the preorganization of monomer shape by restricting bond rotations about all backbone dihedral angles has been demonstrated to be useful for de novo design of peptoid structures. Such design strategies are hitherto unexplored for β-peptoids; to date, no preorganized β-peptoid monomers have been reported. Here, we report the first design strategy for β-peptoids, in which all four backbone dihedral angles (ω, ϕ, θ, ψ) are rotationally restricted on a per-residue basis. The introduction of a cyclopentane constraint realized the preorganized monomer structure and led to a β-peptoid with a stable twisted strand shape.