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Updated: Jul 5, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
Published on: July 31, 2010
Investigation of the interaction between colloidal TiO(2) and bovine hemoglobin using spectral methods
Yan-Qing Wang1, Hong-Mei Zhang, Rong-Hua Wang
1Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng City, People's Republic of China. wyqing76@126.com
Abstract:
The interaction between bovine hemoglobin (BHb) and TiO(2) colloid was investigated by UV/vis absorption, UV/vis diffuse reflectance spectrum, IR, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. TiO(2) effectively quenched the intrinsic fluorescence of BHb via static quenching. The process of binding TiO(2) on BHb was a spontaneous molecular interaction procedure. The thermodynamic parameters, DeltaH degrees and DeltaS degrees were estimated to be -78.07 kJ mol(-1), -110.93 J mol(-1)K(-1) according to the van' Hoff equation. This indicates that the van der Waals and hydrogen bonds interactions played a major role in stabilizing the TiO(2)-BHb complex. The effect of TiO(2) on the conformation of BHb was analyzed using synchronous fluorescence spectroscopy.
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