ACETYLATED HUMAN ALBUMIN AS CHIRAL SELECTOR IN HPLC - RESOLUTION OF RACEMIC DRUGS AND PROTEIN-BINDING STUDIES

Selective acetylation of Lysine 199 in human serum albumin anchored to a HPLC silica matrix has been performed by in situ reaction with aspi rin. This modification, which is reported to occur under physiological conditions, influences the affinity of solutes to the protein anti th en the chromatographic retention and enantioselectivity of a wide rang e of compounds. The retention was significantly shorter and the enanti oselectivity was enhanced for some of the solutes, the chromatographic performance resulting then improved. The modification of HSA affects the binding behaviour of drugs either lo the warfarin-phenylbutazone b inding area (also know as site I) and to the indole-benzodiazepines bi nding area (also know as site II).