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Comparative study of the binding of 3 flavonoids to the fat mass and obesity‐associated protein by spectroscopy and molecular modeling
Author(s) -
Zhang Lijiao,
Ren Ting,
Wang Zechun,
Wang Ruiyong,
Chang Junbiao
Publication year - 2017
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2606
Subject(s) - naringenin , apigenin , quercetin , chemistry , binding constant , fluorescence spectroscopy , quenching (fluorescence) , hydrogen bond , flavonoid , molecular model , photochemistry , biophysics , fluorescence , molecule , biochemistry , binding site , organic chemistry , biology , physics , quantum mechanics , antioxidant
Abstract This study aims to investigate the interaction between 3 flavonoids (quercetin, apigenin, and naringenin) and fat mass and obesity‐associated protein by fluorescence, ultraviolet‐visible absorption spectroscopy, and molecular modeling. Results indicate that the intrinsic fluorescence of fat mass and obesity‐associated protein can be quenched by the 3 flavonoids through a static quenching procedure. Thermodynamic analysis and molecular modeling results suggest that hydrophobic interaction and hydrogen bond forces play the major roles in the binding process. Moreover, results also show that the rank order of quenching constant and binding constant is quercetin > apigenin > naringenin.

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