THE CONFORMATIONAL-ANALYSIS OF PEPTIDES USING FOURIER-TRANSFORM IR SPECTROSCOPY

THE CONFORMATIONAL-ANALYSIS OF PEPTIDES USING FOURIER-TRANSFORM IR SPECTROSCOPY
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DOI:
10.1002/bip.360370404
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发表时间:
1995-01-01
期刊:
影响因子:
2.9
通讯作者:
CHAPMAN, D
CHAPMAN, D
中科院分区:
生物学4区
文献类型:
--
作者:
HARIS, PI;CHAPMAN, D

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傅里叶变换红外光谱(FTIR)可用于广泛环境中肽的构象分析。可以在水溶液、有机溶剂、洗涤剂胶束以及磷脂膜中进行测量。肽的二级结构信息可以从强酰胺I带的分析中获得。脂质双层基质内的二级结构元素的取向可以通过偏振衰减全反射-FTIR光谱法来确定。氢-氘交换可以通过分析酰胺II带来监测。本文综述了用FTIR光谱研究多肽体系的一些实例。对含丙甲霉素和α-氨基异丁酸的肽的研究表明,FTIR光谱是鉴定3(10)-螺旋结构的灵敏工具。在与带电的脂质相互作用后的爪蟾抗菌肽的结构的变化,检测上升的FTIR光谱。鲎素是含有膜活性肽的β折叠的一个例子。偏振it光谱揭示了鲎素的反平行β-折叠结构平行于膜表面取向。合成对应于大蛋白质的功能/结构重要区域的肽变得越来越流行,FTIR光谱已用于分析对应于电压门控钾通道的离子选择性孔的合成肽的结构。在生物膜系统中,这些肽采用高度螺旋结构。在这些肽聚集的条件下,也可以检测到一些分子间β折叠结构的存在。(C)John Wiley & Sons,Inc.
Fourier transform infrared spectroscopy (FTIR) can be used for conformational analysis of peptides in a wide range of environments. Measurements can be performed in aqueous solution, organic solvents, detergent micelles as well as in phospholipid membranes. Information on the secondary structure of peptides can be derived from the analysis of the strong amide I band. Orientation of secondary, structural elements within a lipid bilayer matrix can be determined by means of polarized attenuated total reflectance-FTIR spectroscopy. Hydrogen-deuterium exchange can be monitored by the analysis of the amide II band. This review gives some example of peptide systems studied by FTIR spectroscopy. Studies on alamethicin and alpha-aminoisobutyric acid containing peptides have shown that FTIR spectroscopy is a sensitive tool for identifying 3(10)-helical structures. Changes in the structure of the magainins upon interaction with charged lipids were detected rising FTIR spectroscopy. Tachyplesin is an example of a beta-sheet containing membrane active peptide. Polarized it spectroscopy reveals that the antiparallel beta-sheet structures of tachyplesin are oriented parallel to the membrane surface. Synthesis of peptides corresponding to functionally/structurally important regions of large proteins is becoming increasingly popular FTIR spectroscopy has been used to analyze the structure of synthetic peptides corresponding to the ion-selective pore of the voltage-gated potassium channel. In biomembrane systems these peptides adopt a highly helical structure. Under conditions, where these peptides are aggregated the presence of some intermolecular beta-sheet structure can also be detected. (C) 1995 John Wiley & Sons, Inc.