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result sql = This paper was designed to investigate the interaction of ethyl maltol with human serum albumin (HSA) under physiological condition by fluorescence, synchronous fluorescence, three-dimensional fluorescence, Fourier transformation infrared spectra, and molecular docking method. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of HSA by ethyl maltol was static quenching mechanism. The binding constants of ethyl maltol-HSA complexes were observed to be 2.59, 1.88, 1.54, 1.13×10(4)M(-1) at 289, 296, 303 and 310K, respectively. The thermodynamic parameters, ?H(0) and ?S(0) were calculated to be -28.61kJmol(-1) and -14.59Jmol(-1)K(-1). Energy transfer from tryptophan to ethyl maltol occurred by a FRET mechanism, and the donor-acceptor distance (3.04nm) had been determined according to Förster's theory. Molecular docking studies revealed that ethyl maltol situated within subdomain IIA (site I) of HSA. Fluorescence displacement experiments also proved the binding sites between ethyl maltol and HSA.
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result sql = The investigation of the binding behavior between ethyl maltol and human serum albumin by multi-spectroscopic methods and molecular docking.
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result sql = This paper was designed to investigate the interaction of ethyl maltol with human serum albumin (HSA) under physiological condition by fluorescence, synchronous fluorescence, three-dimensional fluorescence, Fourier transformation infrared spectra, and molecular docking method. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of HSA by ethyl maltol was static quenching mechanism. The binding constants of ethyl maltol-HSA complexes were observed to be 2.59, 1.88, 1.54, 1.13×10(4)M(-1) at 289, 296, 303 and 310K, respectively. The thermodynamic parameters, ?H(0) and ?S(0) were calculated to be -28.61kJmol(-1) and -14.59Jmol(-1)K(-1). Energy transfer from tryptophan to ethyl maltol occurred by a FRET mechanism, and the donor-acceptor distance (3.04nm) had been determined according to Förster's theory. Molecular docking studies revealed that ethyl maltol situated within subdomain IIA (site I) of HSA. Fluorescence displacement experiments also proved the binding sites between ethyl maltol and HSA.
Publication: 2012 May 24 ;96C:316-323.
Publication Date: 2012 May 24
Study Author(s): Yue, Yuanyuan;Liu, Jianming;Yao, Meihuan;Yao, Xiaojun;Fan, Jing;Ji, Hanxuan;
Institution: School of Chemistry and Environmental Science, Henan Key Laboratory for Environmental Pollution Control, Key Laboratory for Yellow River and Huai River Water Environmental and Pollution Control, Ministry of Education, Henan Normal University, Xinxiang, Henan 453007, PR China.
Shortcut link to this study:
Publication Date: 2012 May 24
Study Author(s): Yue, Yuanyuan;Liu, Jianming;Yao, Meihuan;Yao, Xiaojun;Fan, Jing;Ji, Hanxuan;
Institution: School of Chemistry and Environmental Science, Henan Key Laboratory for Environmental Pollution Control, Key Laboratory for Yellow River and Huai River Water Environmental and Pollution Control, Ministry of Education, Henan Normal University, Xinxiang, Henan 453007, PR China.
Shortcut link to this study:
This paper was designed to investigate the interaction of ethyl maltol with human serum albumin (HSA) under physiological condition by fluorescence, synchronous fluorescence, three-dimensional fluorescence, Fourier transformation infrared spectra, and molecular docking method. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of HSA by ethyl maltol was static quenching mechanism. The binding constants of ethyl maltol-HSA complexes were observed to be 2.59, 1.88, 1.54, 1.13×10(4)M(-1) at 289, 296, 303 and 310K, respectively. The thermodynamic parameters, ?H(0) and ?S(0) were calculated to be -28.61kJmol(-1) and -14.59Jmol(-1)K(-1). Energy transfer from tryptophan to ethyl maltol occurred by a FRET mechanism, and the donor-acceptor distance (3.04nm) had been determined according to Förster's theory. Molecular docking studies revealed that ethyl maltol situated within subdomain IIA (site I) of HSA. Fluorescence displacement experiments also proved the binding sites between ethyl maltol and HSA.
PMID: 22705675
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