Cover Feature: A Chemical Biology Approach to Understanding Molecular Recognition of Lipid II by Nisin(1-12): Synthesis and NMR Ensemble Analysis of Nisin(1-12) and Analogues (Chem. Eur. J. 64/2019)
Cover Feature: A Chemical Biology Approach to Understanding Molecular Recognition of Lipid II by Nisin(1-12): Synthesis and NMR Ensemble Analysis of Nisin(1-12) and Analogues (Chem. Eur. J. 64/2019)
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封面专题：了解乳链菌肽 (1-12) 对脂质 II 分子识别的化学生物学方法：乳链菌肽 (1-12) 和类似物的合成和 NMR 整体分析（Chem. Eur. J. 64/2019）
DOI：
10.1002/chem.201903848
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发表时间：
2019
期刊：
影响因子：
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通讯作者：
Dickman R
中科院分区：
文献类型：
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作者：
Dickman R
脂质II识别：合成lantibiotic乳链菌肽的双环N-末端区域（残基1-12）的类似物。为了分析肽的该区域如何与其靶标（脂质II的焦磷酸部分）结合，进行了野生型肽和合成类似物之一的NMR系综分析。这表明两个环在一定程度上是预先组织好的，可以与焦磷酸基团结合。在连接两个环的中心酰胺键中表现出的高度柔性使得两个环能够在“开放”结构和能够结合焦磷酸的“笼”之间切换。更多信息可以在M的论文全文中找到。Erdélyi，AB塔博尔等人，第14572页。
Lipid II recognition: Analogues of the bicyclic N-terminal region of the lantibiotic nisin, residues 1–12, were synthesised. In order to analyse how this region of the peptide binds to its target, the pyrophosphate moiety of lipid II, NMR ensemble analysis of the wild-type peptide and one of the synthetic analogues was carried out. This revealed that the two rings are pre-organised to an extent for binding to the pyrophosphate group. A high degree of flexibility exhibited in the central amide bond joining the two rings enables the two rings to switch between an “open” structure and a “cage” capable of binding to the pyrophosphate. More information can be found in the Full Paper by M. Erdélyi, AB Tabor et al. on page 14572.