Author/Authors :
Guillaume De Nanteuil، نويسنده , , Philippe Gloanec، نويسنده , , Christine Lila-Ambroise، نويسنده , , Bernard Portevin، نويسنده , , Alain Boudon، نويسنده , , Alain Rupin، نويسنده , , Tony J. Verbeuren، نويسنده ,
Abstract :
Structural variations of P2 and P3 residues in tripeptidic boroarginine thrombin inhibitors led to compounds with similar potency than reference compound DuP 714, but with enhanced selectivity for thrombin compared to plasmin.
Replacement of the P2 proline residue in tripeptidic thrombin inhibitors by non natural amino acids (PHI, ABO, N-cycloalkyl glycines) afforded compounds with similar potency than reference compound DuP 714, but with enhanced selectivity for thrombin as compared to plasmin.
