Preparation of dextran-bound recombinant hirudin and its pharmacokinetic behaviour
Research article published in Biomedica biochimica acta (1990)
Abstract
Recombinant desulphatohirudin was bound via lysine residues to oxidized dextrans. The hirudin-dextran conjugates inhibit thrombin like free hirudin. The Ki-values are in the same range. In rabbits and rats the pharmacokinetic behaviour following i.v. administration of these conjugates was examined in comparison to that of hirudin. The hirudin-dextran conjugates were more slowly eliminated than hirudin, the distribution volumes in steady-state were significantly reduced, and, in comparison to hirudin, 5 to 15 times larger areas under the plasma concentration-time-curves were obtained.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Summary
Preparation of dextran-bound recombinant hirudin and its pharmacokinetic behaviour.
Why This Matters for Hirudotherapy
This study examined recombinant desulphatohirudin chemically conjugated to oxidized dextrans via lysine residues and its pharmacokinetic behavior after intravenous administration in rabbits and rats. The conjugates inhibited thrombin with Ki-values in the same range as free hirudin, while showing slower elimination, significantly reduced steady-state distribution volumes, and 5- to 15-fold larger areas under the plasma concentration-time curves compared with unconjugated hirudin. For ASH's domain, the relevance is indirect: hirudin is the potent thrombin inhibitor originally characterized from the medicinal leech, and the work illustrates a formulation strategy for prolonging its circulatory exposure. However, the compound studied is recombinant desulphatohirudin bound to dextran rather than a native leech-secretome component, the study is limited to animal pharmacokinetics, and no therapeutic efficacy or safety data are provided.
Citation
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