title: Methylation of genistein and kaempferol improves their affinities for proteins.
abstract: Methylation of flavonoids appears to be a simple and effective way to improve metabolic resistance and transport of flavonoids. Serum albumins are major soluble proteins serving as transport proteins for many exogenous compounds. This work in here mainly concerns about the effect of methylation of flavonoids on the affinity for human serum albumin (HSA) and ovalbumin. One isoflavone (genistein) and one flavonol (kaempferol) and their monomethylated derivatives at position 4' (biochanin A and kaempferide) were studied for their affinities for ovalbumin and HSA. The methylation of flavonoids significantly affects the binding process. In general, the methylation of flavonoids improved the affinities for proteins by 2-16 times. This result supports that the methylation of genistein and kaempferol enhanced the transporting ability, which leads to facilitated absorption and greatly increased bioavailability. The methylation increases the hydrophobicity of genistein and kaempferol, and the hydrophobic interaction plays an important role in binding flavonoids to HSA and ovoalbumin.
authors: School of Chemistry and Chemical Engineering, Xinglin College, Nantong University, Nantong, PR China. hui_cao0830@yahoo.cn
authors: Hui
authors: H
authors: Cao
authors: Xiaohui
authors: X
authors: Jing
authors: Donghui
authors: D
authors: Wu
authors: Yujun
authors: Y
authors: Shi
mesh_terms: D001682:Biological Availability; D001692:Biological Transport; D019833:Genistein / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007408:Intestinal Absorption; D044949:Kaempferols / Q000378:metabolism*; D008745:Methylation; D010047:Ovalbumin / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*
chemical_list: D044949:Kaempferols; D012709:Serum Albumin; C449720:kaempferide; C006552:kaempferol; D010047:Ovalbumin; D019833:Genistein; C004541:biochanin A