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Thomas Bitter, Mercedes Lpez, Goetz Nowak

Design and characterization of dipetacompinR10H, a dipetalogastin II-derived, classical competitive thrombin inhibitor

Keywords: Thrombin inhibitor, Dipetalogastin, rational drug design, chimeric protein, classical competitive kinetics

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.

Thrombosis and Haemostasis, Schattauer

Print ISSN: 0340-6245
Volume: 97, 01/2007
Pages: 139 - 145

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