Direct liquid chromatographic separation of enantiomers on immobilized protein stationary phases. III. Optical resolution of a series of N-aroyl d,l-amino acids by high-performance liquid chromatography on bovine serum albumin covalently bound to silica

Abstract

A series of N-aroyl d,l-amino acids was investigated with respect to direct optical resolution by high-performance liquid affinity chromatography on a stationary phase consisting of bovine serum albumin covalently bound to a 10-μm silica support. In all instances the k′ values increased with decreasing pH of the mobile phase. Many of the compounds, such as the N-benzoyl and N-naphthoyl derivatives of d,l-alanine and,d,l-phenylalanine, could be completely resolved into the optical antipodes. The 2-substituent of the amino acid was found to exert a great influence not only on the degree of resolution but also on the elution order of the enantiomers. A change in the N-aroyl substituent from a benzoyl to a 2-naphthoyl group caused a large increase in the retention of both enantiomers of a d,l-alanine derivative. © 1983.