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Binding site for basic drugs on alpha 1-acid glycoprotein as revealed by chemometric analysis of biochromatographic
R Kaliszan1, A Nasal, M Turowski
1Department of Biopharmaceutics and Pharmacodynamics, Medical University, Gdańsk, Poland.
Abstract:
Interactions between alpha 1-acid glycoprotein (AGP) and 52 basic drugs were quantified by means of high-performance liquid chromatography (HPLC). The HPLC retention parameters were related quantitatively to the hydrophobicity and molecular modelling parameters, giving rise to the prediction of relative drug-AGP binding from the chemical structure of a drug. A structural model of one binding site on AGP, common for various classes of drugs, was defined which accounted for the observed and reported differences in binding to AGP. A combination of biochromatography and chemometrics has been presented as a promising new approach in biochemical/pharmacological studies.