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[The reaction mechanism between ofloxacin and bovine serum albumin].

Yi Pg, Yu Qs, Shang Zc, Zong Hx

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Abstract

AIM: To study the reaction mechanism between ofloxacin and bovine serum albumin (BSA) in aqueous solution. METHODS: Fluorescence spectra and microcalorimetry was used. RESULTS: The binding constant K was found to be 1.20 x 10(5) L.mol-1 and the number of binding site n was 1.20. Microcalorimetric measurements showed that the molar enthalpy change was delta rHm approximately 0 for the reaction. The effect of ofloxacin on the conformation of BSA was analyzed using synchronous fluorescence spectrometry. The binding distance (r = 2.59 nm) and transfer efficiency (E = 0.38) between ofloxacin and BSA were also obtained according to the theory of Forster's non-radiation energy transfer. CONCLUSION: The interaction between ofloxacin and BSA is stronger and the main binding force is hydrophobic interactions.

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What this paper is about

AIM: To study the reaction mechanism between ofloxacin and bovine serum albumin (BSA) in aqueous solution. METHODS: Fluorescence spectra and microcalorimetry was used. RESULTS: The binding constant K was found to be 1.20 x 10(5) L.mol-1 and the number of binding site n was 1.20. Microcalorimetric measurements showed that the molar enthalpy change was delta rHm approximately 0 for the reaction. The effect of ofloxacin on the conformation of BSA was analyzed using synchronous fluorescence spectrometry. The binding distance (r = 2.59 nm) and transfer efficiency (E = 0.38) between ofloxacin and BSA were also obtained according to the theory of Forster's non-radiation energy transfer. CONCLUSION: The interaction between ofloxacin and BSA is stronger and the main binding force is hydrophobic interactions.

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Available abstract

AIM: To study the reaction mechanism between ofloxacin and bovine serum albumin (BSA) in aqueous solution. METHODS: Fluorescence spectra and microcalorimetry was used. RESULTS: The binding constant K was found to be 1.20 x 10(5) L.mol-1 and the number of binding site n was 1.20. Microcalorimetric measurements showed that the molar enthalpy change was delta rHm approximately 0 for the reaction. The effect of ofloxacin on the conformation of BSA was analyzed using synchronous fluorescence spectrometry. The binding distance (r = 2.59 nm) and transfer efficiency (E = 0.38) between ofloxacin and BSA were also obtained according to the theory of Forster's non-radiation energy transfer. CONCLUSION: The interaction between ofloxacin and BSA is stronger and the main binding force is hydrophobic interactions.

Key concepts: Isothermal microcalorimetry, Ofloxacin, Chemistry, Bovine serum albumin, Binding constant, Enthalpy, Aqueous solution, Fluorescence

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