Characterization of interactions between polyphenolic compounds and human serum proteins by capillary electrophoresis

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 studie...

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Published in:Analytical and bioanalytical chemistry 2008-05, Vol.391 (2), p.625-632
Main Authors: Diniz, Andréa, Escuder-Gilabert, Laura, Lopes, Norberto P., Villanueva-Camañas, Rosa María, Sagrado, Salvador, Medina-Hernández, María José
Format: Article
Language:English
Subjects:
Analytical Chemistry
Biochemistry
Characterization and Evaluation of Materials
Chemistry
Chemistry and Materials Science
Electrophoresis, Capillary - methods
Flavonoids - chemistry
Flavonoids - metabolism
Food Science
Humans
Laboratory Medicine
Monitoring/Environmental Analysis
Original Paper
Orosomucoid - chemistry
Orosomucoid - metabolism
Phenols - chemistry
Phenols - metabolism
Polyphenols
Protein Binding
Serum Albumin - metabolism
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Summary: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.
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-008-2046-4