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2013•Chinese Journal of Spectroscopy LaboratoryRequires access

Interactions Between Cefotaxime Sodium and Bovine Serum Albumin

Lan Gong

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Abstract

The interaction of cefotaxime sodium and bovine serum albumin(BSA) was studied by fluorescence spectroscopy,synchronous fluorescence spectroscopy and UV spectra.The results showed that the cefotaxime sodium evidently quenched intrinsic fluorescence of BSA,static quenching was main,both molar ratio was 1:l,and the binding constants were 1.20X 10~4(298K),7.63×10~3 L ? mol~(-1)(308K) and 6.69×10~3(313K)L ? mol~(-1),respectively.The Van der Waals force and hydrogen bonding are mainly acting force between cefotaxime sodium and BSA according to the thermodynamic parameters of cefotaxime sodium and BSA.The binding distance r between cefotaxime sodium and BSA is 3.26nm based on the energy transfer theory of non-radiative for Foester.The synchronous fluorescence spectra showed that the conformation of BSA was changed by cefotaxime sodium.

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What this paper is about

The interaction of cefotaxime sodium and bovine serum albumin(BSA) was studied by fluorescence spectroscopy,synchronous fluorescence spectroscopy and UV spectra.The results showed that the cefotaxime sodium evidently quenched intrinsic fluorescence of BSA,static quenching was main,both molar ratio was 1:l,and the binding constants were 1.20X 10~4(298K),7.63×10~3 L ? mol~(-1)(308K) and 6.69×10~3(313K)L ? mol~(-1),respectively.The Van der Waals force and hydrogen bonding are mainly acting force between cefotaxime sodium and BSA according to the thermodynamic parameters of cefotaxime sodium and BSA.The binding distance r between cefotaxime sodium and BSA is 3.26nm based on the energy transfer theory of non-radiative for Foester.The synchronous fluorescence spectra showed that the conformation of BSA was changed by cefotaxime sodium.

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Available abstract

The interaction of cefotaxime sodium and bovine serum albumin(BSA) was studied by fluorescence spectroscopy,synchronous fluorescence spectroscopy and UV spectra.The results showed that the cefotaxime sodium evidently quenched intrinsic fluorescence of BSA,static quenching was main,both molar ratio was 1:l,and the binding constants were 1.20X 10~4(298K),7.63×10~3 L ? mol~(-1)(308K) and 6.69×10~3(313K)L ? mol~(-1),respectively.The Van der Waals force and hydrogen bonding are mainly acting force between cefotaxime sodium and BSA according to the thermodynamic parameters of cefotaxime sodium and BSA.The binding distance r between cefotaxime sodium and BSA is 3.26nm based on the energy transfer theory of non-radiative for Foester.The synchronous fluorescence spectra showed that the conformation of BSA was changed by cefotaxime sodium.

Key concepts: Cefotaxime, Chemistry, Bovine serum albumin, Hydrogen bond, van der Waals force, Sodium, Quenching (fluorescence), Fluorescence

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