Effect of the glycosylation of flavonoids on interaction with protein |
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Authors: | Hui Cao Donghui Wu Hongxian Wang Ming Xu |
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Affiliation: | aSchool of Chemistry and Chemical Engineering, Nantong University, Nantong, Jiangsu 226007, PR China;bDepartment of Radiation Oncology, Memorial Sloan-Kettering Cancer Center, NY 10021, USA |
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Abstract: | In this paper, two flavonoid aglycones (baicalein, quercetin) and their glycosides (baicalin, quercitrin) were studied for their ability to bind protein by quenching the protein intrinsic fluorescence. From the spectra obtained, the bimolecular quenching constants, the apparent static binding constants, and binding sites values were calculated. The glycosylation of flavonoids decreases the binding affinity with protein. For quercetin and quercitrin, the binding constants for BSA were 3.65 × 107 and 6.47 × 103 L mol−1, respectively. For baicalein and baicalin, the binding constants were 4.54 × 108 and 1.63 × 106 L mol−1, respectively. |
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Keywords: | BSA Flavonoid Glycosylation Interaction Fluorescence quenching |
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