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Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin
- Source :
-
Journal of Molecular Structure . Aug2009, Vol. 931 Issue 1-3, p55-59. 5p. - Publication Year :
- 2009
-
Abstract
- Abstract: The mutual interaction of riboflavin (RF) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under simulative physiological conditions. The fluorescence quenching mechanism of BSA by RF should belong to dynamic quenching according to the Stern–Volmer equation, but also the effect of ground complex formation and energy transfer could not be completely precluded in BSA–RF system. The binding constants and the corresponding thermodynamic parameters at different temperatures were calculated, which indicated the presence of hydrophobic forces between RF and BSA. The averaged binding distance between riboflavin and BSA was also obtained based on the theory of FÖrster’s non-radiation energy transfer. Moreover, the effect of riboflavin on the conformation of BSA was analyzed using synchronous fluorescence. The effects of some common ions Cu2+, Zn2+, Ca2+, and Mg2+ on the binding constant between riboflavin and BSA were also examined. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00222860
- Volume :
- 931
- Issue :
- 1-3
- Database :
- Academic Search Index
- Journal :
- Journal of Molecular Structure
- Publication Type :
- Academic Journal
- Accession number :
- 43311657
- Full Text :
- https://doi.org/10.1016/j.molstruc.2007.06.035