Destabilase
Lysozyme with isopeptidase activity that dissolves stabilized fibrin clots — including aged thrombi resistant to tPA.
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Lysozyme with isopeptidase activity that dissolves stabilized fibrin clots — including aged thrombi resistant to tPA.
- Evidence level
- In vitro
- Drug vs leech
- Purified natural compound
- Safety domains
- Bleeding
Clinical translation limit
Destabilase's reported fibrinolytic activity in vitro and in limited animal studies does NOT establish clinical efficacy as a thrombolytic agent. No FDA-approved derivative exists; whole-leech therapy is not approved for any thromboembolic indication.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 12,500 Da
- Source species
- Hirudo medicinalis
- Discovered
- 1986 · Baskova et al.
- PDB structures
- 6OJ9
Biological Targets
- → isopeptide ε-(γ-Glu)-Lys bonds in cross-linked fibrin
Key Citations
- Baskova IP, Nikonov GI (1991), Blood Coagul Fibrinolysis · PMID 1772985
- Kurdyumov AS, Manuvera VA, Baskova IP, Lazarev VN (2015), BMC Biochem · PMID 26589324
External Resources
Related Fibrinolytic Compounds
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.
Destabilase-2
Second isoform of destabilase — lysozyme / isopeptidase activity targeting cross-linked fibrin.