title: Structure-inhibitory activity relationship of plasmin and plasma kallikrein inhibitors.
abstract: 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.
authors.affiliation: Faculty of Pharmaceutical Sciences, Kobe Gakuin University, Kobe, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Tsuda
authors.forename: M
authors.initials: M
authors.lastname: Tada
authors.forename: K
authors.initials: K
authors.lastname: Wanaka
authors.forename: U
authors.initials: U
authors.lastname: Okamoto
authors.forename: A
authors.initials: A
authors.lastname: Hijikata-Okunomiya
authors.forename: S
authors.initials: S
authors.lastname: Okamoto
authors.forename: Y
authors.initials: Y
authors.lastname: Okad
mesh_terms: D000588:Amines / Q000737:chemistry; D000818:Animals; D002417:Cattle; D004791:Enzyme Inhibitors / Q000737:chemistry*; D005341:Fibrinolysin / Q000737:chemistry*; D005342:Fibrinolysis; D006801:Humans; D020842:Plasma Kallikrein / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry; D014568:Urokinase-Type Plasminogen Activator / Q000737:chemistry
chemical_list: D000588:Amines; D004791:Enzyme Inhibitors; D020842:Plasma Kallikrein; D014357:Trypsin; D013917:Thrombin; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator; C008699:octylamine