Accession Number : ADP008540

Title :   Synthesis and Anti-Elastase Activity of Amide-Cyclized Peptide Analogs of Alpha1-Antitrypsin,

Corporate Author : WATERLOO UNIV (ONTARIO)

Personal Author(s) : Crivici, Anna ; Lajoie, Gilles

Report Date : 1992

Pagination or Media Count : 2

Abstract : The serine protease inhibitor a1-antitrypsin is the most potent inhibitor of human leukocyte elastase (HLE). The mechanism of inhibition of HLE by a 1-AT has not been clearly defined. We have synthesized linear and side-chain cyclized peptide analogs of the reactive site region of this natural inhibitor in an attempt to mimic its bioactive conformation. The alpha-AT analogs 1-3 enclose the reactive site within a loop defined by an amide bond between glutamic acid and lysine side chains, while peptides are cyclized to stabilize either an alpha-helix or a bend in the enzyme binding region N-terminal to the reactive site.

Descriptors :   *PEPTIDE HYDROLASES, *ENZYME INHIBITORS, TRYPSIN, PEPTIDES, LEUKOCYTES, SYNTHESIS(CHEMISTRY), CANADA.

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE