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Russian Journal of General Chemistry

, Volume 80, Issue 8, pp 1710–1717 | Cite as

Studies of the interaction between apigenin and bovine serum albumin by spectroscopic methods

  • Yonghui Shang
  • Hua Li
Article

Abstract

The interaction between apigenin (Ap) and bovine serum albumin (BSA) in physiological buffer (pH = 7.4) is investigated by fluorescence quenching technique and UV-vis absorption spectra. The results reveal that Ap could strongly quench the intrinsic fluorescence of BSA. The quenching mechanism of Ap for BSA varies with the change of Ap concentration. when Ap concentration is lower, it is a static quenching procedure, when Ap concentration is higher, a combined quenching (both static and dynamic) would operate. The apparent binding constants Ka and number of binding sites n of Ap with BSA are obtained by fluorescence quenching method. The thermodynamic parameters, enthalpy change (Δr H m and entropy change (Δr S m ), are calculated to be −15.382 kJ mol−1 K−1 < 0 and 104.888 J mol−1 K−1 > 0, respectively, which indicate that the interaction of Ap with BSA is driven mainly by hydrogen bonding and hydrophobic interactions. The distance r between BSA and Ap is calculated to be 1.89 nm based on Förster’s non-radiative energy transfer theory. The results of synchronous fluorescence spectra show that binding of Ap with BSA cannot induce conformational changes in BSA.

Keywords

Bovine Serum Albumin General Chemistry Apigenin Intrinsic Fluorescence Static Quenching 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Pleiades Publishing, Ltd. 2010

Authors and Affiliations

  1. 1.Institute of Analytical Science, School of Chemistry and Material ScienceNorthwest UniversityXi’anPR China
  2. 2.Department of ChemistryXianyang Normal CollegeXianyangPR China

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