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Fluorescence Spectrophotometry tanshinoneA Microemulsion and Bovine Serum Albumin
PAGE \* MERGEFORMAT 12
Fluorescence Spectrophotometry tanshinoneA Microemulsion and Bovine Serum Albumin
Of: Wu Yi, Sun Yue, Panxu Xu, Zhou Jinmei, Chen Zhibin
[Abstract] Objective tanshinone A Microemulsion and the interaction behavior of bovine serum albumin. Methods fluorescence spectrometry, calculated through the Stern Volmer fluorescence quenching data and the binding constant, by calculating the thermodynamic data of tanshinone A and bovine serum albumin interaction mechanism. Results at room temperature with constant 1.93 104 L moL-1, and the binding constant, quenching constant decreases with increasing temperature both, thermodynamic data H0, S0 and G0 are negative. Conclusion Micro emulsion, tanshinone A on the quenching mechanism of bovine serum albumin complex is a static quenching process, the binding mechanism may be van der Waals force and hydrogen bonding.
[Keywords:] tanshinone A; bovine serum albumin; micro-emulsion; binding
Abstract: Objective To study the interaction between tanshinone A and bovine serum albumin (BSA) in the microemulsion system by fluorometry.Methods The binding constant KA was calculated by Stern Volmer equation, The enthalpy variation (H0), Gibbs free energy variation (G0) and entropy variation (S0) were used to explore the interaction mechanism of tanshinone A and BSA.Results The binding constant KA was 1.93 104 L mol-1 at 293 K, the quenching constant and the binding constant both decreased with the increase of temperature, the values of H0, S0 and G0 were all negative. Conclusion It was found that the binding of tanshinone A to BSA in microemulsion system might be concerned with van der Waals force and hydrogen bonding force.
Keywords:: Tanshinone A; bovine serum albumin; microemulsion; binding
Drug interaction between small molecules and biological macromolecules of the chemical and life sciences hot topic. Of serum proteins and endogenous compounds and methods of drug interactions, flu
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