Journal
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
Volume 337, Issue 1-3, Pages 102-108Publisher
ELSEVIER
DOI: 10.1016/j.colsurfa.2008.12.003
Keywords
Hemoglobin; Fe3O4 colloid; Fluorescence spectroscopy; Binding constant
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Funding
- Natural Science Foundation of Education Department of Jiangsu Provinc [07KJA18017]
- Educational Bureau [07KJD150235]
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The interaction between bovine hemoglobin (BHb) and Fe3O4 colloid was investigated by UV/vis absorption, FR-IR, fluorescence, resonance light scattering spectra, CD, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. Fe3O4 effectively quenched the intrinsic fluorescence of BHb via static quenching. The process of binding Fe3O4 on BHb was a spontaneous molecular interaction procedure. The thermodynamic parameters indicate that van der Waals and hydrogen bonds, electrostatic interactions played a major role in stabilizing the Fe3O4-BHb complex. The effect of Fe3O4 on the conformation of BHb was analyzed using CD and synchronous fluorescence spectroscopy. (c) 2008 Elsevier B.V. All rights reserved.
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