Title of article
New tripeptidic thrombin inhibitors. Influence of P2 and P3 residues on activity and selectivity Original Research Article
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 ,
Issue Information
روزنامه با شماره پیاپی سال 1995
Pages
6
From page
1019
To page
1024
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.
Journal title
Bioorganic and Medicinal Chemistry
Serial Year
1995
Journal title
Bioorganic and Medicinal Chemistry
Record number
1300501
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