Abstract
Synthetic peptides corresponding to segments of heparin cofactor II, fibrinogen, thrombomodulin, and hirudin were identified that inhibit thrombin's clotting of fibrinogen without blocking the enzyme's active site. Thrombin activity was inhibited 50% by the following peptide concentrations, with numbers in parentheses indicating residues in the protein sequence: heparin cofactor II(54–75), 38 μM; heparin cofactor II(49–75), 28 μM; fibrinogen γB-chain(410–427), 130 μM; thrombomodulin(426–444), 140 μM; hirudin(54–65), 1.3 μM; hirudin(54–75)SO 4, 0.17 μM. All of these peptides are likely to bind to thrombin's anion-binding exosite, suggesting that this site has broad sequence specificity such that it may participate in many of thrombin's interactions with physiological substrates and inhibitors.
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