Effect of the glycosylation of flavonoids on interaction with protein.
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 x 10(7) and 6.47 x 10(3)L mol(-1), respectively. For baicalein and baicalin, the binding constants were 4.54 x 10(8) and 1.63 x 10(6)L mol(-1), respectively.
Cao
Hui
H
School of Chemistry and Chemical Engineering, Nantong University, Nantong, Jiangsu 226007, PR China. hui_cao0830@yahoo.cn
Wu
Donghui
D
Wang
Hongxian
H
Xu
Ming
M
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D044950:Flavanones / Q000737:chemistry / Q000378:metabolism*; D005419:Flavonoids / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D015394:Molecular Structure; D011485:Protein Binding; D011794:Quercetin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D044950:Flavanones; D005419:Flavonoids; D012710:Serum Albumin, Bovine; C012526:quercitrin; C038044:baicalin; C006680:baicalein; D011794:Quercetin