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Helical self-assembly of an unusual pseudopeptide: crystallographic evidence
Zeitschrift für Kristallographie - Crystalline Materials ( IF 1.2 ) Pub Date : 2023-10-28 , DOI: 10.1515/zkri-2023-0034
Arpita Dutta 1 , Suven Das 2 , Purak Das 2
Affiliation  

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.

中文翻译:

一种不寻常的伪肽的螺旋自组装:晶体学证据

伪肽是一类多功能的有机构建模块,在广泛的领域具有潜在的应用。在当前的研究中,N 和 C 末端受保护合成了基于丙氨酸的短伪肽,其中 5-氨基间苯二甲酸 (5-AIA)(一种刚性非蛋白性 γ-氨基丁酸)作为 C 端残基掺入。单晶 X 射线分析表明[0013] -上述肽的丙氨酸残基采用φψ聚脯氨酸 II 构象的特征值。伪肽的自组装似乎代表了通过 NH⋯O、CH⋯O 氢键和 π-π 相互作用形成的超分子螺旋结构。
更新日期:2023-10-28
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