In situ ATR-IR spectroscopy study of adsorbed protein: Visible light denaturation of bovine serum albumin on TiO2

被引：84
作者：
Bouhekka, A. [1 ,2 ,3 ]
Buergi, T. [1 ]
机构：
[1] Dept Chim Phys, CH-1211 Geneva 4, Switzerland
[2] Univ Oran Es Senia, Lab Phys Couches Minces & Mat Elect, Oran 31100, Algeria
[3] Univ Hassiba Ben Bouali, Dept Phys, Chlef 02000, Algeria
来源：
APPLIED SURFACE SCIENCE | 2012年 / 261卷
关键词：
In situ spectroscopy; TiO2; Visible light; BSA adsorption; Denaturation; Protein structure; REFLECTION INFRARED-SPECTROSCOPY; WATER H2O SOLUTIONS; SECONDARY STRUCTURE; PEPTIDE COMPOUNDS; BLOCKING-AGENTS; ADSORPTION; SURFACE; PHOTOCATALYSIS; SPECTROPHOTOMETRY; POLYPEPTIDES;
D O I：
10.1016/j.apsusc.2012.08.017
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
In this work in situ Fourier transform infrared-attenuated total reflection (FTIR-ATR) spectroscopy in a flow-through cell was used to study the effect of visible light irradiation on bovine serum albumin (BSA) adsorbed on porous TiO2 films. The experiments were performed in water at concentrations of 10(-6) mol/l at room temperature. The curve fitting method of the second derivative spectra allowed us to explore details of the secondary structure of pure BSA in water and conformation changes upon adsorption as well as during and after illumination by visible light. The results clearly show that visible light influences the conformation of adsorbed BSA. The appearance of a shift of the amide I band, in the original spectra, from 1653 cm(-1) to 1648 cm(-1), is interpreted by the creation of random coil in the secondary structure of adsorbed BSA. The second derivative analysis of infrared spectra permits direct quantitative analysis of the secondary structural components of BSA, which show that the percentage of alpha-helix decreases during visible light illumination whereas the percentage of random coil increases. (C) 2012 Elsevier B. V. All rights reserved.
引用
收藏
页码：369 / 374
页数：6
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