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  • Title: Structure-inhibitory activity relationship of plasmin and plasma kallikrein inhibitors.
    Author: Tsuda Y, Tada M, Wanaka K, Okamoto U, Hijikata-Okunomiya A, Okamoto S, Okad Y.
    Journal: Chem Pharm Bull (Tokyo); 2001 Nov; 49(11):1457-63. PubMed ID: 11724238.
    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.
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