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Binding site for basic drugs on α 1 ‐acid glycoprotein as revealed by chemometric analysis of biochromatographic data
Author(s) -
Kaliszan Roman,
Nasal Antoni,
Turowski Maciej
Publication year - 1995
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1130090504
Subject(s) - chemistry , chemometrics , chromatography , high performance liquid chromatography , orosomucoid , glycoprotein , drug , biochemistry , pharmacology , medicine
Interactions between α 1 ‐acid glycoprotein (AGP) and 52 basic drugs were quantified by means of highperformance 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.