HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHIC SCREENING METHODS FOR REVEALING THE STEREOSELECTIVITY OF REVERSIBLE INTERACTIONS BETWEEN LIGAND ENANTIOMERS AND A COUNTERPART SUBSTANCE

The stereoselectivity of the reversible binding interaction between tryptophan enantiomers and various counterpart substances (oligo- and polysaccharides, proteins) has been studied by HPLC. The properties of the ,,simplest'' of three different experimental designs are presented. Bovine serum albumin bound to silica gel was used as the chiral HPLC stationary phase; phosphate-buffered DL-tryptophan solution was used as mobile phase. The stereoselectivity of interactions between different oligo- and macrobiomolecules and the two tryptophan enantiomers was evaluated from the areas of negative recorder deflections at the retention times of the D and L isomers of tryptophan.