Synthetic peptide inhibitors of complement serine proteases--I. Identification of functionally equivalent protease inhibitor sequences in serpins and inhibition of C1s and D.
Sequence homology comparisons between serum serine protease inhibitors led to the prediction that the C-terminal sequences are functionally equivalent and represent an essential protease binding domain. Inhibition of complement serine protease D cleavage of factor B and of C1s cleavage of C4 by synthetic peptides containing sequences from the C-termini of three serum serine protease inhibitors supports this prediction. These functionally equivalent peptides represent a new class of inhibitors of D and C1s as well as other serum serine proteases.
Glover
G I
GI
Biological Sciences Department, Monsanto Company, St. Louis, MO 63198.
Schasteen
C S
CS
Liu
W S
WS
Levine
R P
RP
D000595:Amino Acid Sequence; D003167:Complement Activation; D003174:Complement C1 Inactivator Proteins; D011416:Complement Factor D / Q000037:antagonists & inhibitors; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000494:pharmacology*; D015842:Serine Proteinase Inhibitors; D013329:Structure-Activity Relationship
D003174:Complement C1 Inactivator Proteins; D010446:Peptide Fragments; D015842:Serine Proteinase Inhibitors; D011416:Complement Factor D