Binding site for basic drugs on alpha 1-acid glycoprotein as revealed by chemometric analysis of biochromatographic data.
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.
Kaliszan
R
R
Department of Biopharmaceutics and Pharmacodynamics, Medical University, Gdańsk, Poland.
Nasal
A
A
Turowski
M
M
D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D009961:Orosomucoid / Q000737:chemistry* / Q000378:metabolism; D011955:Receptors, Drug / Q000737:chemistry* / Q000378:metabolism; D012822:Silicon Dioxide; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship
D009961:Orosomucoid; D011955:Receptors, Drug; D012822:Silicon Dioxide