dansylproline and norvaline

The enantioselective binding sites on bovine serum albumin were examined by HPLC using 19 racemic 5-N, N-dimethylamino-1-naphthalenesulfonyl derivatives of alpha-amino acids (dansyl amino acids) as chiral probes. On a bovine serum albumin bonded chiral stationary phase, seven L-forms eluted faster than their D-forms, while ten D-forms eluted before their L-forms. It was speculated that either two classes or two different binding sites exist on bovine serum albumin which can be distinguished by N-dansyl-L-proline and N-dansyl-D-norvaline. This was confirmed by fluorometric experiments where non-fluorescent 1-naphthalenesulfonyl derivatives were synthesized and competitive adsorption experiments were performed.

Topics: Amino Acids; Binding Sites; Binding, Competitive; Chromatography, High Pressure Liquid; Dansyl Compounds; Naphthalenesulfonates; Proline; Serum Albumin, Bovine; Spectrometry, Fluorescence; Stereoisomerism; Valine; Warfarin