Minimal structural requirements for agonist activity of PAR-2 activating peptides
| Autor: | Elisa Perissutti, Beatrice Severino, Giuseppe Cirino, Vincenzo Santagada, Giuseppe Caliendo, Carla Cicala, Ferdinando Fiorino, Vincenzo De Filippis |
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| Přispěvatelé: | Santagada, Vincenzo, Caliendo, Giuseppe, Severino, Beatrice, Perissutti, Elisa, Fiorino, Ferdinando, Cicala, Carla, De Filippis, V, Cirino, Giuseppe |
| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: |
Agonist
Male medicine.drug_class Clinical Biochemistry Drug Evaluation Preclinical Pharmaceutical Science Peptide Arginine Biochemistry Muscle Smooth Vascular PAR-2 Receptor chemistry.chemical_compound Structure-Activity Relationship Leucine Drug Discovery Peptide synthesis medicine Potency Animals Receptor PAR-2 Rats Wistar Receptor Molecular Biology agonist Aorta chemistry.chemical_classification Dipeptide Molecular Structure Organic Chemistry Thrombin Dipeptides Transmembrane protein In vitro Rats chemistry Drug Design Molecular Medicine Receptors Thrombin |
| Popis: | Protease-activated receptor 2 (PAR-2) is involved in inflammatory, gastrointestinal, and vascular diseases. The aim of the present work was to elucidate the minimal structural features for PAR-2 agonist activity in short peptides. Our study resulted in the discovery of dipeptide derivatives of N α -benzoyl-Arg(NO 2 )-Leu-NH 2 displaying a potency comparable to that of the full-length rat PAR-2 activating peptide (Ser-Leu-Ile-Gly-Arg-Leu-NH 2 ). |
| Databáze: | OpenAIRE |
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