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Using Fluorinated Amino Acids for Structure Analysis of Membrane-Active Peptides by Solid-State ~(19)F-NMR

机译:含氟氨基酸通过固态〜(19)F-NMR分析膜活性肽的结构

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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-CF3-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.
机译:用多种氟化氨基酸标记几种不同的膜活性肽,以通过固态〜(19)F NMR进行结构分析。即,使用4-F-Phg / 4-CF_3-Phg,3,3,3-F_3-Ala / 3-F-Ala和2-CF3-Ala代替单个氨基酸,例如Ile / Leu,分别不显着干扰肽的构象或功能的Ala和Aib。可以分析这些NMR报告基团,以计算脂质双层中肽的结构和迁移率。这篇综述着重于〜(19)F标记氨基酸的合成挑战,例如外消旋作用和氟的消除,并且将总结模型膜中各种抗菌肽和融合肽的最新研究结果。

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