Volume 30, Issue 6 e2606
RESEARCH ARTICLE

Comparative study of the binding of 3 flavonoids to the fat mass and obesity-associated protein by spectroscopy and molecular modeling

Lijiao Zhang

Lijiao Zhang

College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou, China

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Ting Ren

Ting Ren

College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou, China

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Zechun Wang

Zechun Wang

College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou, China

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Ruiyong Wang

Corresponding Author

Ruiyong Wang

College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou, China

Correspondence

Ruiyong Wang and Junbiao Chang, College of Chemistry and Molecular Engineering, Zhengzhou University, 100 Science Avenue, Zhengzhou 450001, China.

Email: [email protected]; [email protected]

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Junbiao Chang

Corresponding Author

Junbiao Chang

College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou, China

Correspondence

Ruiyong Wang and Junbiao Chang, College of Chemistry and Molecular Engineering, Zhengzhou University, 100 Science Avenue, Zhengzhou 450001, China.

Email: [email protected]; [email protected]

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First published: 06 January 2017
Citations: 28

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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