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Issue 9, 2014
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Study on the interaction characteristics of dexamethasone sodium phosphate with bovine serum albumin by spectroscopic technique

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Abstract

The interaction of dexamethasone sodium phosphate (DEX-P) with bovine serum albumin (BSA) was studied by fluorescence quenching in combination with UV-Vis spectroscopic method under near physiological conditions. Fluorescence quenching rate constants and binding constants for BSA–DEX-P system were determined at different temperatures. The fluorescence quenching of BSA by DEX-P was due to static quenching and energy transfer. The results of thermodynamic parameters, ΔH (−161.0 kJ mol−1), ΔS (−468.0 J mol−1 K−1) and ΔG (−21.54 to −16.86 kJ mol−1), indicated that van der Waals interaction and hydrogen bonding played a major role in DEX-P–BSA association. Competitive experiments demonstrated that the primary binding site of DEX-P on BSA was located at site III in sub-domain IIIA of BSA. The distance between BSA and DEX-P was estimated to be 1.23 nm based on the Förster resonance energy transfer theory. The binding constant (Ka) of BSA–DEX-P at 298 K was 2.239 × 104 L mol−1. Circular dichroism spectra, synchronous fluorescence and three-dimensional fluorescence studies showed that the presence of DEX-P could change the conformation of BSA during the binding process.

Graphical abstract: Study on the interaction characteristics of dexamethasone sodium phosphate with bovine serum albumin by spectroscopic technique

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Publication details

The article was received on 05 Mar 2014, accepted on 04 Jun 2014 and first published on 05 Jun 2014


Article type: Paper
DOI: 10.1039/C4NJ00327F
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Citation: New J. Chem., 2014,38, 4092-4098

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    Study on the interaction characteristics of dexamethasone sodium phosphate with bovine serum albumin by spectroscopic technique

    Q. Wang, X. Liu, M. Su, Z. Shi and H. Sun, New J. Chem., 2014, 38, 4092
    DOI: 10.1039/C4NJ00327F

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