Accession Number:

ADP008540

Title:

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

Descriptive Note:

Corporate Author:

WATERLOO UNIV (ONTARIO)

Personal Author(s):

Report Date:

1992-01-01

Pagination or Media Count:

2.0

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.

Subject Categories:

  • Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE