Abstract：Interaction of Sunset yellow (SY) and β-carotene (BC) with bovine serum albumin (BSA) was investigated under simulated physiological conditions by spectroscopic approaches (fluorescence, UV-Vis, FT-IR and CD). Both SY and BC quenched the intrinsic fluorescence of BSA through static quenching mechanism. The thermodynamic parameters (DH, DS, and DG) obtained from the fluorescence data measured at three different temperatures indicated that the binding of SY to BSA involved electrostatic force, and that of BC to BSA mainly by hydrogen bonding and van der Waals forces. The binding sites number n and binding constants Ka were also obtained. The result of FT-IR spectra and CD showed that the binding of SY to BSA induced conformational changes in BSA.
张方圆, 倪永年. 日落黄和β-胡萝卜素与牛血清白蛋白相互作用的对比研究[J]. 化学学报, 2012, 70(12): 1379-1384.
Zhang Fangyuan, Ni Yongnian. A Comparison Study on the Interaction of Sunset Yellow and β-Carotene with Bovine Serum Albumin. Acta Chimica Sinica, 2012, 70(12): 1379-1384.