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Thromb Haemost 2007; 97(01): 139-145
DOI: 10.1160/TH06-06-0308
DOI: 10.1160/TH06-06-0308
New Technologies, Diagnostic Tools and Drugs
Design and characterization of dipetacompinR10H, a dipetalogastin II-derived, classical competitive thrombin inhibitor
Further Information
Publication History
Received
06 June 2006
Accepted after resubmission
05 November 2006
Publication Date:
28 November 2017 (online)
Summary
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 Ki 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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