Fluorine–hydrogen interactions observed in a helix structure having an orn-free gramicidin S sequence incorporating 4-trans-fluoroproline

IF 0.5 Q4 CRYSTALLOGRAPHY

Acta Crystallographica Section E: Crystallographic Communications Pub Date : 2025-04-01 DOI:10.1107/S2056989025002592

Asano Akiko , Mizuki Sakata , Kato Takuma , Mitsunobu Doi

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引用次数: 0

Abstract

Decapeptide having a gramicidin S sequence forms a helix structure supported by a fluorine–H interaction.

The decapeptide Boc-(d-Phe-tFPro-Val-Leu-Leu)₂—OMe (1) (Boc is tert-butoxycarbonyl, tFPro is 4-trans-fluoro-l-proline d-Phe is d-phenylalanine, Val is valine and Leu is leucine) crystallized in a methanol-solvated form (C₆₈H₁₀₄F₂N₁₀O₁₃·CH₄O). Peptide 1 has a sequence similar to gramicidin S (GS) incorporating tFPro. GS is a cyclic peptide, with the d-Phe-Pro unit known as a strong β-turn inducer in previous studies. Thus, it was initially assumed that 1 would bend at the d-Phe6-tFPro7 position, potentially forming a sheet-like structure. However, the structure of 1 was a helix, a surprising finding in GS-related structural studies. A factor enabling this helical formation could be the fluorine–H interactions between tFPro and the aromatic rings of d-Phe residues.

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在含有4-反式氟脯氨酸的无麦杀草蛋白S序列的螺旋结构中观察到氟-氢相互作用

具有革兰杀菌素S序列的十肽形成由氟- h相互作用支撑的螺旋结构。十肽Boc-(d-Phe-tFPro-Val-Leu-Leu) 2-OMe (1) （Boc为叔丁基氧羰基，tFPro为4-反式氟-l-脯氨酸，d-Phe为d-苯基丙氨酸，Val为缬氨酸，Leu为亮氨酸）在甲醇溶剂化形式（C68H104F2N10O13·ch40）中结晶。肽1具有与含有tFPro的gramicidin S （GS）相似的序列。GS是一种环状肽，其d-Phe-Pro单元在以前的研究中被称为强β-转诱导剂。因此，最初假设1会在d-Phe6-tFPro7位置弯曲，可能形成片状结构。然而，1的结构是螺旋结构，这在gs相关的结构研究中是一个令人惊讶的发现。导致这种螺旋形成的一个因素可能是tFPro和d-Phe残基芳香环之间的氟- h相互作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Acta Crystallographica Section E: Crystallographic Communications Chemistry-Chemistry (all)

CiteScore

1.90

自引率

0.00%

发文量

351

审稿时长

3 weeks

期刊介绍： Acta Crystallographica Section E: Crystallographic Communications is the IUCr''s open-access structural communications journal. It provides a fast, simple and easily accessible publication mechanism for crystal structure determinations of inorganic, metal-organic and organic compounds. The electronic submission, validation, refereeing and publication facilities of the journal ensure rapid and high-quality publication of fully validated structures. The primary article category is Research Communications; these are peer-reviewed articles describing one or more structure determinations with appropriate discussion of the science.

Fluorine–hydrogen inter­actions observed in a helix structure having an orn-free gramicidin S sequence incorporating 4-trans-fluoro­proline

Abstract

Fluorine–hydrogen interactions observed in a helix structure having an orn-free gramicidin S sequence incorporating 4-trans-fluoroproline