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2007•Chinese Journal of Applied ChemistryRequires access

Spectroscopic Study on the Interaction of Furbenicillin Sodium with Bovine Serum Albumin

Yang Zhao

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Abstract

Bonding reaction of Furbenicillin Sodium(FBS) with bovine serum albumin(BSA) was studied by means of UV-Vis,fluorescence and infrared spectroscopy.The experimental results suggest that there is strong interaction between FBS and BSA,and FBS has a strong quenching effect on the BSA fluorescence.It is confirmed from fluorescence data that the quenching effect of FBS on the BSA fluorescence is a single static quenching process.The fluorescence quenching data was analyzed using the Stern-Volmer equation and double-logarithm equation.The binding constant and binding sites were 1.04×105 and 1.09 at ambient temperature(26 ℃),respectively.It is revealed from the above results that the bonding of FBS with BSA leads to a significant change of the secondary structure of BSA.

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What this paper is about

Bonding reaction of Furbenicillin Sodium(FBS) with bovine serum albumin(BSA) was studied by means of UV-Vis,fluorescence and infrared spectroscopy.The experimental results suggest that there is strong interaction between FBS and BSA,and FBS has a strong quenching effect on the BSA fluorescence.It is confirmed from fluorescence data that the quenching effect of FBS on the BSA fluorescence is a single static quenching process.The fluorescence quenching data was analyzed using the Stern-Volmer equation and double-logarithm equation.The binding constant and binding sites were 1.04×105 and 1.09 at ambient temperature(26 ℃),respectively.It is revealed from the above results that the bonding of FBS with BSA leads to a significant change of the secondary structure of BSA.

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Available abstract

Bonding reaction of Furbenicillin Sodium(FBS) with bovine serum albumin(BSA) was studied by means of UV-Vis,fluorescence and infrared spectroscopy.The experimental results suggest that there is strong interaction between FBS and BSA,and FBS has a strong quenching effect on the BSA fluorescence.It is confirmed from fluorescence data that the quenching effect of FBS on the BSA fluorescence is a single static quenching process.The fluorescence quenching data was analyzed using the Stern-Volmer equation and double-logarithm equation.The binding constant and binding sites were 1.04×105 and 1.09 at ambient temperature(26 ℃),respectively.It is revealed from the above results that the bonding of FBS with BSA leads to a significant change of the secondary structure of BSA.

Key concepts: Chemistry, Bovine serum albumin, Quenching (fluorescence), Fluorescence, Analytical Chemistry (journal), Fluorescence spectroscopy, Sodium, Binding constant

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