SELECTIVE INHIBITORS OF PLASMA KALLIKREIN

Based on a tetrapeptide fragment [Pro(387)-Ser(390)] of HK we have dev eloped a series of potent low molecular weight (5-600 Da) inhibitors o f PK which are stable to the enzyme. These inhibitors show good select ivity for PK versus tissue kallikrein, thrombin and plasmin. Such inhi bitors will help define the role of PK and kinins in human physiology and pathophysiology. They may also find clinical use in the treatment of diseases where kinins are important mediators.