Abstract:

The threedimensional spectra combined with fluorescence spectroscopy under simulative physiological conditions were used to investigate the interaction between resveratrol and human serum albumin. With the presence of Tris-HCl, the endogenous fluorescence was quenched by resveratrol and the three-dimensional spectra also changed when resveratrol exsited in the system. The synchronous fluorescence intensity and the concentration of serum albumin solution have a good linear relationship. A new synchronous fluorescence method for the determination of trace proteins was developed. The spectral characterization and intensity of synchronous fluorescence were related to the value of Δλ, reaction medium and so on. Under optimized conditions, the fluorescence intensity(I) of the system was proportional to the concentration of protein in the range of 1.380~276.0 mg/L, with the detection limit of 1.037 mg/L for human serum albumin(HSA). This method was applied to the determination of proteins in human serum, urine and saliva samples and the recovery was 93.5%~105.8%. The results obtained with this method were accordant with those obtained by the coomassie brilliant blue(G-250) method.

Key words: resveratrol, human serum albumin, synchronous fluorescence spectra, coomassie brilliant blue, three-dimensional fluorescence