ABSTRACT
The interaction of ten natural polyphenolic compounds (chlorogenic acid, apigenin, catechin, epicatechin, flavanone, flavone, quercetin, rutin, vicenin-2 and vitexin) with human serum albumin and mixtures of human serum albumin and α(1)-acid glycoprotein under near physiological conditions is studied by capillary electrophoresis-frontal analysis. Furthermore, the binding of these polyphenolic compounds to total plasmatic proteins is evaluated using ultrafiltration and capillary electrophoresis. In spite of the relatively small differences in the chemical structures of the compounds studied, large differences were observed in their binding behaviours to plasmatic proteins. The hydrophobicity, the presence/absence of some functional groups, steric hindrance and spatial arrangement seem to be key factors in the affinity of natural polyphenols towards plasmatic proteins.
Subject(s)
Electrophoresis, Capillary/methods , Flavonoids/metabolism , Orosomucoid/metabolism , Phenols/metabolism , Serum Albumin/metabolism , Flavonoids/chemistry , Humans , Orosomucoid/chemistry , Phenols/chemistry , Polyphenols , Protein BindingABSTRACT
This paper points out the usefulness of biopartitioning micellar chromatography (BMC) using capillary columns as a high-throughput primary screening tool providing key information about the oral absorption, skin permeability, and brain-blood distribution coefficients of 15 polyphenols (6 flavones, 2 flavonols, a flavanone, 2 flavan-3-ols, 3 phenolic acids, and a phloroglucinol) in a simple and economical way. For the compounds studied, except vicenin-2, rutin, chlorogenic acid, p-hydroxycinnamic acid, and 4-hydroxybenzoic acid, maximal oral absorption (>90%) can be expected, if there are not solubility problems or metabolic processes. On the other hand, the most retained compounds in BMC, that is, 5-hydroxyflavone, flavone, and flavanone, show the highest brain-blood distribution coefficients and skin permeability coefficients.