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Studies on the Interaction of Sophordine with Bovine Serum Albumin

Xiuxia Chen

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Abstract

The interaction of sophordine with bovine serum albumin(BSA)was investigated by fluorescence quenching,fluorescence anisotropy,and UV-vis absorbance under the simulative physiological condition.Fluorescence quenching data showed that the interaction of sophordine with BSA formed a new complex,the quenching mechanism belonged to static fluorescence quenching.The binding constants were obtained at 292,298,304 and 310 K to be 1.219×106,1.164×106,1.110×106 and 1.057×106 L/mol,respectively.The thermodynamic parameters,enthalpy change(ΔH)and entropy change(ΔS)were calculated to be-5.97 kJ/mol and 96.11 J/(mol·K)via van't Hoff equation,which indicated that the interaction between sophordine and BSA was driven mainly by electrostatic force.The competitive probes,such as warfarin and ibuprofen(site I and site II probes,respectively),revealed that the binding location of sophordine to BSA in the site I of the hydrophobic pocket.

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What this paper is about

The interaction of sophordine with bovine serum albumin(BSA)was investigated by fluorescence quenching,fluorescence anisotropy,and UV-vis absorbance under the simulative physiological condition.Fluorescence quenching data showed that the interaction of sophordine with BSA formed a new complex,the quenching mechanism belonged to static fluorescence quenching.The binding constants were obtained at 292,298,304 and 310 K to be 1.219×106,1.164×106,1.110×106 and 1.057×106 L/mol,respectively.The thermodynamic parameters,enthalpy change(ΔH)and entropy change(ΔS)were calculated to be-5.97 kJ/mol and 96.11 J/(mol·K)via van't Hoff equation,which indicated that the interaction between sophordine and BSA was driven mainly by electrostatic force.The competitive probes,such as warfarin and ibuprofen(site I and site II probes,respectively),revealed that the binding location of sophordine to BSA in the site I of the hydrophobic pocket.

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Available abstract

The interaction of sophordine with bovine serum albumin(BSA)was investigated by fluorescence quenching,fluorescence anisotropy,and UV-vis absorbance under the simulative physiological condition.Fluorescence quenching data showed that the interaction of sophordine with BSA formed a new complex,the quenching mechanism belonged to static fluorescence quenching.The binding constants were obtained at 292,298,304 and 310 K to be 1.219×106,1.164×106,1.110×106 and 1.057×106 L/mol,respectively.The thermodynamic parameters,enthalpy change(ΔH)and entropy change(ΔS)were calculated to be-5.97 kJ/mol and 96.11 J/(mol·K)via van't Hoff equation,which indicated that the interaction between sophordine and BSA was driven mainly by electrostatic force.The competitive probes,such as warfarin and ibuprofen(site I and site II probes,respectively),revealed that the binding location of sophordine to BSA in the site I of the hydrophobic pocket.

Key concepts: Bovine serum albumin, Chemistry, Quenching (fluorescence), Fluorescence, Enthalpy, Absorbance, Fluorescence anisotropy, Hydrophobic effect

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