Biopartitioning micellar chromatoraphy to predict blood to lung, blood to liver, blood to fat and blood to skin partition coefficients of drugs

[EN] Biopartitioning micellar chromatography (BMC), a mode of micellar liquid chromatography that uses micellar mobile phases of Brij35 in adequate experimental conditions, has demonstrated to be useful in mimicking the drug partitioning process into biological systems. In this paper, the usefulness of BMC for predicting the partition coefficients from blood to lung, blood to liver. blood to fat and blood to skin is demonstrated. PLS2 and multiple linear regression (MLR) models based on BMC retention data are proposed and compared with other ones reported in bibliography. The proposed models present better or similar descriptive and predictive capability. (C) 2008 Elsevier B.V. All rights reserved.The authors acknowledge the Spanish Ministry of Science and Technology (MCYT) and the European Regional Development Fund (ERDF) for the financial support (Project SA2005-01435).Martin-Biosca, Y.; Torres-Cartas, S.; Villanueva-Camanas, RM.; Sagrado, S.; Medina-Hernandez, MJ. (2009). Biopartitioning micellar chromatoraphy to predict blood to lung, blood to liver, blood to fat and blood to skin partition coefficients of drugs. Analytica Chimica Acta. 632(2):296-303. doi:10.1016/j.aca.2008.11.004S296303632

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 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