Study of the interaction between a new Schiff-base complex and bovine serum albumin by fluorescence spectroscopy.
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 Förster's non-radiation energy transfer theory.
Xiang
Yanling
Y
Department of Chemistry and Center of Analysis and Testing, Nanchang University, Nanchang 330031, Jiangxi, PR China.
Wu
Fangying
F
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D006801:Humans; D006834:Hydrazines / Q000737:chemistry; D015394:Molecular Structure; D012545:Schiff Bases / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D015032:Zinc / Q000737:chemistry
D006834:Hydrazines; D012545:Schiff Bases; D012710:Serum Albumin, Bovine; D015032:Zinc