title: Mass spectrometry reveals elastase inhibitors from the reactive centre loop of alpha1-antitrypsin.
abstract: 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.
authors.affiliation: The Oxford Centre for Molecular Sciences, UK.
authors.forename: P A
authors.initials: PA
authors.lastname: Wright
authors.forename: A A
authors.initials: AA
authors.lastname: Rostom
authors.forename: C V
authors.initials: CV
authors.lastname: Robinson
authors.forename: C J
authors.initials: CJ
authors.lastname: Schofield
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D013058:Mass Spectrometry; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D013552:Swine; D000515:alpha 1-Antitrypsin / Q000737:chemistry*
chemical_list: D004791:Enzyme Inhibitors; D000515:alpha 1-Antitrypsin; D010196:Pancreatic Elastase