ecallantide and octylamine

ecallantide has been researched along with octylamine* in 1 studies

Other Studies

1 other study(ies) available for ecallantide and octylamine

Article	Year
Structure-inhibitory activity relationship of plasmin and plasma kallikrein inhibitors. Chemical & pharmaceutical bulletin, 2001, Volume: 49, Issue:11 Based on the structure of Tra-Tyr(O-Pic)-octylamide, a portion of the octylamine was replaced with moieties bearing hydrophobic, basic or acidic groups. Replacement of the C-terminal residue with a moiety bearing a hydrophobic group gave the proper affinity of the inhibitor to both plasmin (PL) and plasma kallikrein (PK). While addition of a basic residue did not improve the affinity of the inhibitor, a carboxylic acid attached to the phenyl ring increased the PK selectivity of the inhibitor. Topics: Amines; Animals; Cattle; Enzyme Inhibitors; Fibrinolysin; Fibrinolysis; Humans; Plasma Kallikrein; Structure-Activity Relationship; Thrombin; Trypsin; Urokinase-Type Plasminogen Activator	2001

Article

Year

Structure-inhibitory activity relationship of plasmin and plasma kallikrein inhibitors.

Chemical & pharmaceutical bulletin, 2001, Volume: 49, Issue:11

Based on the structure of Tra-Tyr(O-Pic)-octylamide, a portion of the octylamine was replaced with moieties bearing hydrophobic, basic or acidic groups. Replacement of the C-terminal residue with a moiety bearing a hydrophobic group gave the proper affinity of the inhibitor to both plasmin (PL) and plasma kallikrein (PK). While addition of a basic residue did not improve the affinity of the inhibitor, a carboxylic acid attached to the phenyl ring increased the PK selectivity of the inhibitor.

Topics: Amines; Animals; Cattle; Enzyme Inhibitors; Fibrinolysin; Fibrinolysis; Humans; Plasma Kallikrein; Structure-Activity Relationship; Thrombin; Trypsin; Urokinase-Type Plasminogen Activator

2001