Spectroscopic studies on the interaction between riboflavin and albumins

被引:127
作者
Zhao Hongwei [1 ]
Ge Min [1 ]
Zhang Zhaoxia [1 ]
Wang Wenfeng [1 ]
Wu Guozhong [1 ]
机构
[1] Chinese Acad Sci, Shanghai Inst Appl Phys, Shanghai 201800, Peoples R China
基金
中国国家自然科学基金;
关键词
riboflavin; albumin; intrinsic fluorescence; fluorescence quenching;
D O I
10.1016/j.saa.2005.12.038
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
The interactions between riboflavin (RF)and human and bovine serum albumin (HSA and BSA) were studied by using absorption and fluorescence spectroscopic methods. Intrinsic fluorescence emission spectra of serum albumin in the presence of RF show that the endogenous photosensitizer acts as a quencher. The decrease of fluorescence intensity at about 350 urn is attributed to changes in the environment of the protein fluorophores caused by the ligand. The quenching mechanisms of albumins by RF were discussed. The binding constants and binding site number were obtained at various temperatures. The distance between albumins and RF in the complexes suggests that the primary binding site for RF is close to tryptophan residue (Trp214) of HSA and Trp212 of BSA. The hydration process of albumins has also been discussed. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:811 / 817
页数:7
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