一种不寻常的假肽的螺旋自组装:晶体学证据

IF 0.9 4区 材料科学 Q3 CRYSTALLOGRAPHY
Arpita Dutta, Suven Das, Purak Das
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引用次数: 0

摘要

摘要假肽是一种多功能的有机构建模块,在广泛的领域具有潜在的应用。本研究合成了N和C端受保护的l -丙氨酸基短假肽,其中C端残基为5-氨基间苯二甲酸(5-AIA),一种刚性的非蛋白质源性γ-氨基丁酸。单晶x射线分析表明,上述肽的l -Ala残基具有聚脯氨酸II构象的φ和ψ值特征。伪肽的自组装似乎通过NH⋯O, CH⋯O氢键和π -π相互作用代表了超分子螺旋结构。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Helical self-assembly of an unusual pseudopeptide: crystallographic evidence
Abstract Pseudopeptides are a versatile class of organic building blocks having potential applications in a wide range of domains. In the current study, N and C termini protected l -alanine based short pseudopeptide was synthesized, where 5-aminoisophthalic acid (5-AIA), a rigid non-proteogenic γ-amino butyric acid was incorporated as C-terminal residue. The single crystal X-ray analysis revealed that the l -Ala residue of the aforesaid peptide adopts ϕ and ψ values characteristic of polyproline II conformation. Self-assembly of the pseudopeptide seems to represent a supramolecular helical architecture via NH⋯O, CH⋯O hydrogen bonding and π–π interactions.
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来源期刊
CiteScore
2.00
自引率
16.70%
发文量
55
期刊介绍: Zeitschrift für Kristallographie – Crystalline Materials was founded in 1877 by Paul von Groth and is today one of the world’s oldest scientific journals. It offers a place for researchers to present results of their theoretical experimental crystallographic studies. The journal presents significant results on structures and on properties of organic/inorganic substances with crystalline character, periodically ordered, modulated or quasicrystalline on static and dynamic phenomena applying the various methods of diffraction, spectroscopy and microscopy.
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