Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 77, Issue 2, Pages 430-436Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2010.06.010
Keywords
Zinc complex of Schiff-base; N '-(2-hydroxynaphthalenemethylene)-4-(2-hydroxylnaphthalenemethylenamine)benzoylhydrazine; Bovine serum albumin; Fluorescence spectroscopy
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Funding
- Natural Science Foundation of China [20965006]
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A new Schiff-base compound, N'-(2-hydroxynaphthalenemethylene)-4-(2-hydroxyl naphthalenemethylenamine)benzoylhydrazine (1), was synthesized and the interaction between zinc complex (1-Zn) and bovine serum albumin (BSA) was investigated by fluorescence and absorption spectroscopies. A marked increase in the fluorescence intensity of 1-Zn was observed at 475 nm upon addition of BSA when excitation wavelength was set at 370 nm in pH 7.4 Tris-HCl buffer solution. Reversely, the intrinsic fluorescence of BSA could be quenched by 1-Zn complex. The quenching mechanism was suggested as static quenching according to the Stern-Volmer equation and the UV-vis absorption spectral change of 1-Zn upon addition of BSA. The binding constants K-b and the number of binding sites n were calculated. The effect of 1-Zn on the conformation of BSA was studied using synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. In addition, the binding average distance r between the donor (BSA) and acceptor (1-Zn) was estimated based on the Forster's non-radiation energy transfer theory. (C) 2010 Elsevier B.V. All rights reserved.
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