Enantioselective binding sites on bovine serum albumin to dansyl amino acids

The enantioselective binding sites on bovine serum albumin were examined by HPLC using 19 racemic 5-N,N-dimethylamino-1-naphthalenesulfonyl derivative s of alpha-amino acids (dansyl amino acids) as chiral probes. On a bovine s erum albumin bonded chiral stationary phase, seven L-forms eluted faster th an their D-forms, while ten D-forms eluted before their L-forms. It was spe culated that either two classes or two different binding sites exist on bov ine serum albumin which can be distinguished by N-dansyl-L-proline and N-da nsyl-D-norvaline. This was confirmed by fluorometric experiments where nonf luorescent 1-naphthalenesulfonyl derivatives were synthesized and competiti ve adsorption experiments were performed. (C) 1999 Elsevier Science B.V. Al l rights reserved.