Recombinant Destabilase (Aged-Clot Variant)
Recombinant H. medicinalis destabilase tested against aged human blood clots resistant to thrombolytics — Bobrovsky 2021 demonstrates dose-response isopeptide-bond cleavage.
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Recombinant H. medicinalis destabilase tested against aged human blood clots resistant to thrombolytics — Bobrovsky 2021 demonstrates dose-response isopeptide-bond cleavage.
- Evidence level
- In vitro
- Drug vs leech
- Recombinant (genetically expressed)
- Safety domains
- Bleeding
Clinical translation limit
Recombinant destabilase's in vitro aged-clot dissolution does NOT establish clinical thrombolytic efficacy. No FDA-approved derivative exists; pilot study results require validation in randomized clinical trials and pharmacokinetic / immunogenicity safety profiling.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 12,500 Da
- Source species
- Hirudo medicinalis
- Discovered
- 2021 · Bobrovsky P et al.
Biological Targets
- → isopeptide ε-(γ-Glu)-Lys bonds in cross-linked / aged fibrin clots
Key Citations
- Bobrovsky P et al. (2021), Curr Issues Mol Biol · PMID 34889897
External Resources
Related Fibrinolytic Compounds
Destabilase
Lysozyme with isopeptidase activity that dissolves stabilized fibrin clots — including aged thrombi resistant to tPA.
Hementerin
Direct fibrinogenolytic enzyme — degrades fibrinogen independently of plasmin.
Hementin
Direct fibrinogenolytic enzyme cleaving fibrinogen alpha-chain at unique sites — independent of plasmin.
Destabilase Isopeptidase Activity
Isopeptidase domain of destabilase that cleaves cross-linked fibrin — distinct from lysozyme domain.