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

Diniz, Andréa ; Escuder-Gilabert, Laura ; Lopes, Norberto P. ; Villanueva-Camañas, Rosa María ; Sagrado, Salvador ; Medina-Hernández, María José

Analytical and bioanalytical chemistry, 2008-05, Vol.391 (2), p.625-632 [Periódico revisado por pares]

Berlin/Heidelberg: Springer-Verlag

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Título:
Characterization of interactions between polyphenolic compounds and human serum proteins by capillary electrophoresis
Autor: Diniz, Andréa ; Escuder-Gilabert, Laura ; Lopes, Norberto P. ; Villanueva-Camañas, Rosa María ; Sagrado, Salvador ; Medina-Hernández, María José
Assuntos: 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
É parte de: Analytical and bioanalytical chemistry, 2008-05, Vol.391 (2), p.625-632
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
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Descrição: 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.
Editor: Berlin/Heidelberg: Springer-Verlag
Idioma: Inglês

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

Diniz, Andréa ; Escuder-Gilabert, Laura ; Lopes, Norberto P. ; Villanueva-Camañas, Rosa María ; Sagrado, Salvador ; Medina-Hernández, María José

Berlin/Heidelberg: Springer-Verlag

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