Direct optical resolution of a series of pharmacologically active racemic sulfoxides by high-performance liquid affinity chromatography.

A series of pharmacologically active racemic sulfoxides was investigated with respect to optical resolution by an affinity chromatographic technique based on enantioselective interactions with immobilized bovine serum albumin. The results show that very small changes in the molecular structure of a drug, at a large distance from the asymmetric center, can drastically alter not only its affinity for the albumin molecule but also the enantioselectivity in the reversible binding process. Apart from being an excellent, rapid method for studies of drug binding to and transport by serum albumins, it has a large potential application as a chromatographic technique for the determination of enantiomeric purity as well as stereoselective uptake processes of drugs.