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  • Title: Design and characterization of dipetacompinR10H, a dipetalogastin II-derived, classical competitive thrombin inhibitor.
    Author: Bitter T, López M, Nowak G.
    Journal: Thromb Haemost; 2007 Jan; 97(1):139-45. PubMed ID: 17200781.
    Abstract:
    The design of small chimeric thrombin inhibitors based on the structure of dipetalogastin II has been previously described. These proteins are effective inhibitors of thrombin showing slow binding or slow, tight-binding kinetics. We report here about dipetacompinR10H, a new dipetalogastin II-derived chimeric thrombin inhibitor, which exhibits classical competitive kinetics. The dissociation constant K (i) of dipetacompinR10H was determined to be 17.1 +/- 0.8 pM. In various coagulation assays it showed a comparable anticoagulant activity like r-hirudin and r-dipetalogastin II. DipetacompinR10H ' s inhibition of thrombin was specific, since no inhibition of other serine proteases like factor Xa, plasmin, trypsin or chymotrypsin has been observed.
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