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Molecular interaction of ctDNA and HSA with sulfadiazine sodium by multispectroscopic methods and molecular modeling
Author(s) -
Geng Shaoguang,
Liu Guosheng,
Li Wei,
Cui Fengling
Publication year - 2013
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2457
Subject(s) - chemistry , human serum albumin , fluorescence , enthalpy , quenching (fluorescence) , fluorescence spectroscopy , molecular model , absorption spectroscopy , spectroscopy , molecular dynamics , binding constant , binding site , analytical chemistry (journal) , chromatography , stereochemistry , computational chemistry , biochemistry , thermodynamics , physics , quantum mechanics
Interactions of sulfadiazine sodium (SD‐Na) with calf thymus DNA (ctDNA) and human serum albumin (HSA) were studied using fluorescence spectroscopy, UV absorption spectroscopy and molecular modeling. The fluorescence experiments showed that the processes were static quenching. The results of UV spectra and molecular modeling of the interaction between SD‐Na and ctDNA indicated that the binding mode might be groove binding. In addition, the interaction of SD‐Na with HSA under simulative physiological conditions was also investigated. The binding constants ( K ) and the number of binding sites ( n ) at different temperatures (292, 302, 312 K) were 5.23 × 10 3 L/mol, 2.18; 4.50 × 10 3 L/mol, 2.35; and 4.08 × 10 3 L/mol, 2.47, respectively. Thermodynamic parameters including enthalpy change (Δ H ) and entropy change (Δ S ) were calculated, the results suggesting that hydrophobic force played a very important role in SD‐Na binding to HSA, which was in good agreement with the molecular modeling study. Moreover, the effect of SD‐Na on the conformation of HSA was analyzed using three‐dimensional fluorescence spectra. Copyright © 2013 John Wiley & Sons, Ltd.