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 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.
Diniz
Andréa
A
Departamento de Ciências Farmacêuticas, CCS, Universidade Estadual de Londrina, Rod. Celso Garcia Cid, PR 445 km 380, CEP 86051-990, Londrina-PR, Brazil.
Escuder-Gilabert
Laura
L
Lopes
Norberto P
NP
Villanueva-Camañas
Rosa María
RM
Sagrado
Salvador
S
Medina-Hernández
María José
MJ
D019075:Electrophoresis, Capillary / Q000379:methods*; D005419:Flavonoids / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009961:Orosomucoid / Q000737:chemistry / Q000378:metabolism*; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D059808:Polyphenols; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*
D005419:Flavonoids; D009961:Orosomucoid; D010636:Phenols; D059808:Polyphenols; D012709:Serum Albumin