Influence of hydroxylation and glycosylation in ring A of soybean isoflavones on interaction with BSA.
In this paper, the influence of hydroxylation and glycosylation of soybean isoflavones in ring A on the interaction with BSA was investigated. Two soybean isoflavone aglycones (daidzein and genistein) and their glycosides (daidzin and genistin) were used to study their ability to bind BSA by quenching the BSA intrinsic fluorescence in solution. The hydroxylation and glycosylation of soybean isoflavones in ring A significantly affected the binding/quenching process; in general, the hydroxylation increases the binding affinity and the glycosylation decreased the binding affinity. For daidzein and daidzin, the binding constants for BSA were 5.2 x 10(4) and 5.58 x 10(3) L mol(-1), respectively. For genistein and genistin, the binding constants were 8.40 x 10(5) and 1.44 x 10(5) L mol(-1), respectively.
Zhao
Jinyao
J
College of Chemistry and Chemical Engineering, Central South University, Changsha 410083, PR China. jyzhaocsu@yahoo.com.cn
Ren
Fenglian
F
D000818:Animals; D001665:Binding Sites; D002021:Buffers; D002417:Cattle; D055598:Chemical Phenomena; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D006900:Hydroxylation; D007529:Isoflavones / Q000737:chemistry* / Q000378:metabolism*; D000432:Methanol / Q000737:chemistry; D015394:Molecular Structure; D009994:Osmolar Concentration; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D012996:Solutions; D013025:Glycine max / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D014325:Tromethamine / Q000737:chemistry; D014867:Water / Q000737:chemistry
D002021:Buffers; D007529:Isoflavones; D012996:Solutions; D014325:Tromethamine; D014867:Water; D012710:Serum Albumin, Bovine; D000432:Methanol