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2015•The Chinese Journal of Clinical PharmacologyRequires access

Study on the combining force of interaction between cefotaxime and bovine serum albumin

Sufen Zhang

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Abstract

Objective To study the interaction between cefotaxime sodium for injection( CTX) and bovine serum albumin( BSA) in tris- HCl buffer of p H 7. 40. Methods The fluorescence intensity of the interaction between BSA and CTX was studied by the fluorescence spectrometry.The fluorescence intensity were analyzed in according to Stern- Volmer equation, double logarithmic equation and thermodynamic equation.Results The fluorescence of BSA was quenched by CTX. At the 299 and 307 K, the quenching rate constant( Kq) was 3. 07 × 1012,3. 48 × 1012L·mol- 1·s- 1,and the binding constant( KA) was 5. 75 ×103,4. 47 × 103 L · mol- 1, respectively. The value of thermodynamic parameters( △G,△H and △S) were less than zero. Conclusion The CTX and BSA formed the ground state complex,and the combining force between CTX and BSA was Van der Waals force and hydrogen bond.

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Objective To study the interaction between cefotaxime sodium for injection( CTX) and bovine serum albumin( BSA) in tris- HCl buffer of p H 7. 40. Methods The fluorescence intensity of the interaction between BSA and CTX was studied by the fluorescence spectrometry.The fluorescence intensity were analyzed in according to Stern- Volmer equation, double logarithmic equation and thermodynamic equation.Results The fluorescence of BSA was quenched by CTX. At the 299 and 307 K, the quenching rate constant( Kq) was 3. 07 × 1012,3. 48 × 1012L·mol- 1·s- 1,and the binding constant( KA) was 5. 75 ×103,4. 47 × 103 L · mol- 1, respectively. The value of thermodynamic parameters( △G,△H and △S) were less than zero. Conclusion The CTX and BSA formed the ground state complex,and the combining force between CTX and BSA was Van der Waals force and hydrogen bond.

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Available abstract

Objective To study the interaction between cefotaxime sodium for injection( CTX) and bovine serum albumin( BSA) in tris- HCl buffer of p H 7. 40. Methods The fluorescence intensity of the interaction between BSA and CTX was studied by the fluorescence spectrometry.The fluorescence intensity were analyzed in according to Stern- Volmer equation, double logarithmic equation and thermodynamic equation.Results The fluorescence of BSA was quenched by CTX. At the 299 and 307 K, the quenching rate constant( Kq) was 3. 07 × 1012,3. 48 × 1012L·mol- 1·s- 1,and the binding constant( KA) was 5. 75 ×103,4. 47 × 103 L · mol- 1, respectively. The value of thermodynamic parameters( △G,△H and △S) were less than zero. Conclusion The CTX and BSA formed the ground state complex,and the combining force between CTX and BSA was Van der Waals force and hydrogen bond.

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

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