Optical Resolution by Liquid Chromatography on Immobilized Bovine Serum Albumin

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Abstract
Direct optical resolution by liquid chromatography based on the enantioselective properties of a protein, particularly bovine serum albumin (BSA), has been shown to be a very versatile method with many useful analytical applications. Although the mechanism of chiral recognition by the protein is largely unknown, some empirically found correlations between retention behaviour and mobile phase composition give a general idea of the main types of solute-protein interactions involved. A summary of results from optical resolution of different classes of racemic compounds is given, together with examples of large substituent effects on retention values.