Using Fluorinated Amino Acids for Structure Analysis of Membrane‐Active Peptides by Solid‐State 19F‐NMR
Using Fluorinated Amino Acids for Structure Analysis of Membrane‐Active Peptides by Solid‐State 19F‐NMR
复制标题
使用氟化氨基酸通过固态 19F-NMR 进行膜活性肽的结构分析
DOI：
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发表时间：
2007
期刊：
影响因子：
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通讯作者：
A. Ulrich
中科院分区：
文献类型：
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作者：
P. Wadhwani;Pierre Tremouilhac;E. Strandberg;S. Afonin;S. Grage;Marco Ieronimo;Marina Berditsch;A. Ulrich
用不同的含氟氨基酸标记了几种不同的膜活性多肽，并用固体~(19)F-核磁共振进行了结构分析。即分别用4-F-PHG/4-CF3-PHG、3，3，3-F3-Ala/3-F-Ala和2-CF3-Ala取代Ile/Leu、Ala和AIB等单一氨基酸，而不显著干扰多肽的构象和功能。可以分析这些核磁共振报告基团来计算该肽在脂双层中的结构和迁移率。本文综述了19种F标记氨基酸的合成挑战，如消旋和去氟，并总结了模型膜中各种抗菌肽和融合多肽的最新研究结果。
Several different membrane-active peptides were labeled with a variety of fluorinated amino acids for structure analysis by solid state 19 F NMR. Namely, 4-F-Phg/4-CF 3 -Phg, 3,3,3-F 3 -Ala/3-F-Ala, and 2-CF 3 -Ala were used to replace a single amino acid such as Ile/Leu, Ala, and Aib, respectively, without significantly perturbing the peptide conformation or function. These NMR reporter groups can be analyzed to calculate the structure and mobility of the peptide in the lipid bilayer. This review focuses on synthetic challenges with 19 F-labeled amino acids, such as racemization and fluorine elimination, and recent results on various antimicrobial and fusogenic peptides in model membranes will be summarized.