Fluorescence spectroscopy and docking study in two flavonoids,isolated tectoridin and its aglycone tectorigenin,interacting with human serum albumin: a comparison study |
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| Authors: | Yuanzhi Li Qing Wang Jiawei He Jin Yan Hui Li |
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| Affiliation: | College of Chemical Engineering, Sichuan University, Chengdu, People's Republic of China |
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| Abstract: | Two flavonoids, tectoridin (TD) isolated from rhizomes of Iris tectorum and hydrolyzed aglycone tectorigenin (TG) were prepared and characterized to compare their different interaction ability with human serum albumin (HSA). Based on the results, the affinity of TG–HSA was stronger than that of TD–HAS, and TG combined more closely with HSA than did TD. HSA fluorescence was quenched by TD/TG. The interactions between TD/TG and HSA involved static quenching. The thermodynamic parameters indicated that both binding processes were spontaneous; hydrogen binding and van der Waals force were the main forces between TD and HSA, whereas a hydrophobic interaction was the main binding force between TG and HSA. Synchronous and 3D fluorescence spectra showed that the binding of TD/TG to HSA induced conformational changes. Moreover, a docking study confirmed the experimental results. Copyright © 2015 John Wiley & Sons, Ltd. |
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| Keywords: | human serum albumin flavonoids tectoridin tectorigenin interaction |
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