 |
|
Title
|
|
Mass spectrometry reveals elastase inhibitors from the reactive centre loop of alpha1-antitrypsin.
|
|
|
Authors
|
|
P.A.Wright,
A.A.Rostom,
C.V.Robinson,
C.J.Schofield.
|
|
|
Ref.
|
|
Bioorg Med Chem Lett, 2000,
10,
1219-1221.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|