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β‐Lactam Derivatives as Enzyme Inhibitors: Carboxy Peptidyl Derivatives of ( S )‐4‐Oxoazetidine‐2‐carboxylate as Peptidomimetics
Author(s) -
Schneider Martin,
Otto HansHartwig
Publication year - 2001
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/1521-4184(200105)334:5<167::aid-ardp167>3.0.co;2-o
Subject(s) - chemistry , peptidomimetic , oligopeptide , stereochemistry , enzyme , carboxylate , lactam , elastase , enzyme inhibitor , carboxylic acid , amino acid , biological activity , peptide , biochemistry , in vitro
4‐Oxoazetidine‐2‐carboxylic acid, protected at the nitrogen by silyl groups, was coupled with amino acid and oligopeptide esters. Desilylation and deprotection of the amino acid residues yielded the free β‐lactam peptides. Structure and properties were elucidated by spectroscopic methods and discussed. Some selected compounds were tested as fibrinogen inhibitors and for thrombocyte aggregation. None of the compounds showed any activity up to a concentration of 10 — 5 Mol/l. Some other compounds exhibited a weak inhibitory activity against elastase (PPE).