Journal
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
Volume 391, Issue 2, Pages 625-632Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-008-2046-4
Keywords
natural polyphenolic compounds; polyphenol-protein interactions; human serum albumin; alpha(1)-acid glycoprotein; whole plasma; frontal analysis; capillary electrophoresis
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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 alpha(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.
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