Chemoenzymatic routes to enantiomerically pure 2-azatyrosine and 2-, 3- and 4-pyridylalanine derivatives

Autor: Patrick Meffre, Valérie Rolland, Amer Moussa, Jean Martinez
Přispěvatelé: Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Université de Nîmes (UNIMES)
Rok vydání: 2011
Předmět:
Zdroj: Amino Acids
Amino Acids, Springer Verlag, 2012, 42, pp.1339-1348. ⟨10.1007/s00726-010-0829-3⟩
ISSN: 1438-2199
0939-4451
DOI: 10.1007/s00726-010-0829-3
Popis: International audience; Enantiomerically pure 2-, 3- or 4-pyridylalanine (pya) and 2-azatyrosine (azatyr) are known to present various biological activities. After incorporation into appropriate peptide sequences, these heterocyclic non natural a-amino acids could behave as new substrates or inhibitors of elastase from Pseudomonas aeruginosa.This enzyme is known to be involved in nosocomial infections and infections related to the cystic fibrosis disease. New efficient chemoenzymatic preparations of those compounds using a-chymotrypsin (a-CT) are presented.
Databáze: OpenAIRE