Compounds > phenylalanyl-prolyl-arginine

phenylalanyl-prolyl-arginine and tartaric-acid

phenylalanyl-prolyl-arginine has been researched along with tartaric-acid* in 1 studies

Other Studies

1 other study(ies) available for phenylalanyl-prolyl-arginine and tartaric-acid

Article	Year
Synthesis of potential thrombin inhibitors. Incorporation of tartaric acid templates as P2 proline mimetics. Bioorganic & medicinal chemistry, 2002, Volume: 10, Issue:5 With the objective to prepare novel non-peptidic thrombin inhibitors, bioisosteres of the inhibitory tripeptide D-Phe-Pro-Arg chain have been examined. Thus, the P1 Arg was replaced with p-amidinobenzylamine, an elongated homologue of the same and with 2,5-dichloro benzylamine. The P2-P3, D-Phe-Pro, was replaced with a novel tartaric acid template coupled to a series of readily available, mainly lipophilic, amines. Some of these compounds exhibit promising thrombin inhibition activity in vitro, IC(50 ) approximately 5.9 microM. Topics: Amines; Anticoagulants; Crystallography, X-Ray; Humans; Inhibitory Concentration 50; Molecular Mimicry; Oligopeptides; Proline; Serine Proteinase Inhibitors; Structure-Activity Relationship; Tartrates; Thrombin	2002

Article

Year

Synthesis of potential thrombin inhibitors. Incorporation of tartaric acid templates as P2 proline mimetics.

Bioorganic & medicinal chemistry, 2002, Volume: 10, Issue:5

With the objective to prepare novel non-peptidic thrombin inhibitors, bioisosteres of the inhibitory tripeptide D-Phe-Pro-Arg chain have been examined. Thus, the P1 Arg was replaced with p-amidinobenzylamine, an elongated homologue of the same and with 2,5-dichloro benzylamine. The P2-P3, D-Phe-Pro, was replaced with a novel tartaric acid template coupled to a series of readily available, mainly lipophilic, amines. Some of these compounds exhibit promising thrombin inhibition activity in vitro, IC(50 ) approximately 5.9 microM.

Topics: Amines; Anticoagulants; Crystallography, X-Ray; Humans; Inhibitory Concentration 50; Molecular Mimicry; Oligopeptides; Proline; Serine Proteinase Inhibitors; Structure-Activity Relationship; Tartrates; Thrombin

2002