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Peptides derived from the reactive centre loop of alpha1-antitrypsin, a serpin, were screened as potential elastase inhibitors by mass spectrometry. An octapeptide, MFLEAIPM, formed a 'stable' ternary complex with porcine elastase: one MFLEAIPM molecule reacted covalently with loss of water, whilst an additional peptide was bound non-covalently. Kinetic analyses suggested that MFLEAIPM may act as an uncompetitive inhibitor and that the activity was associated with the four N-terminal residues.

Type

Journal article

Journal

Bioorg Med Chem Lett

Publication Date

05/06/2000

Volume

10

Pages

1219 - 1221

Keywords

Amino Acid Sequence, Animals, Enzyme Inhibitors, Humans, Kinetics, Mass Spectrometry, Pancreatic Elastase, Swine, alpha 1-Antitrypsin