Mass spectrometry reveals elastase inhibitors from the reactive centre loop of alpha1-antitrypsin.
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.
Wright
P A
PA
The Oxford Centre for Molecular Sciences, UK.
Rostom
A A
AA
Robinson
C V
CV
Schofield
C J
CJ
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*
D004791:Enzyme Inhibitors; D000515:alpha 1-Antitrypsin; D010196:Pancreatic Elastase