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采用傅里叶变换红外光谱和二维红外相关光谱对一些可溶性弹性蛋白进行结构分析。

Structural analysis of some soluble elastins by means of FT-IR and 2D IR correlation spectroscopy.

机构信息

Department of Physical Chemistry of Polymers, Petru Poni Institute of Macromolecular Chemistry, Iasi, Romania.

出版信息

Biopolymers. 2010 Dec;93(12):1072-84. doi: 10.1002/bip.21524.

Abstract

Fourier transform infrared (FT-IR) spectroscopy combined with 2D correlation spectroscopy has been used to offer some information about stability and structure of some soluble elastins. Temperature has been chosen as the perturbation to monitor the infrared behavior of various soluble elastins, namely, α-elastin p, α-elastin, and k-elastin. In the 3800-2700 cm⁻¹ region, the H-containing groups were analyzed. The bonded hydroxyls are found to decrease prior to the NH-related hydrogen bonds and also to the conformational reorganization of hydrocarbon chains. The transition temperatures were evaluated and they were found to agree with those obtained from DSC data. The FTIR spectra and their 2nd derivatives denote that α- elastins exhibited amide-I, -II and -III bands at 1656, 1539 and 1236 cm⁻¹, respectively, while in k-elastin these bands were found at 1652 cm⁻¹ for amide I, 1540 cm⁻¹ for amide II and 1248 cm⁻¹ for amide III. The macroscopic IR finger-print method, which combines: general IR spectra, secondary derivative spectra, and 2D-IR correlation spectra, is useful to discriminate different elastins. Thus using the differences of the position and intensity of the bands from "fingerprint region" of studied elastins, which include the peaks assigned to C==O, C--C groups from α-helix, β-turn, and the peaks assigned to the amide groups, it is possible to identify and discriminate elastins from each others. Furthermore, the pattern of 2D-IR correlation spectra under thermal perturbation, allow their direct identification and discrimination.

摘要

傅里叶变换红外(FT-IR)光谱结合二维相关光谱已被用于提供一些关于某些可溶性弹性蛋白稳定性和结构的信息。选择温度作为扰动来监测各种可溶性弹性蛋白的红外行为,即α-弹性蛋白 p、α-弹性蛋白和 k-弹性蛋白。在 3800-2700cm⁻¹ 区域分析了含 H 基团。发现结合的羟基先于 NH 相关氢键以及烃链的构象重排减少。评估了转变温度,发现它们与从 DSC 数据获得的温度一致。FTIR 光谱及其二阶导数表示,α-弹性蛋白在 1656、1539 和 1236cm⁻¹ 处分别显示酰胺-I、-II 和 -III 带,而在 k-弹性蛋白中,酰胺 I 带位于 1652cm⁻¹,酰胺 II 带位于 1540cm⁻¹,酰胺 III 带位于 1248cm⁻¹。宏观红外指纹方法,结合:一般红外光谱、二阶导数光谱和二维红外相关光谱,可用于区分不同的弹性蛋白。因此,使用从研究弹性蛋白的“指纹区”的带的位置和强度的差异,包括分配给 C==O、C--C 基团的峰,从α-螺旋、β-转角和分配给酰胺基团的峰,可鉴定和区分彼此的弹性蛋白。此外,热扰动下二维红外相关光谱的模式允许它们的直接识别和区分。

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