WpDestabilase
Whitmania pigra destabilase ortholog (Huang 2026) — isopeptidase + clot-destabilizing activity; C-terminal IPATETTTEI deletion enhances isopeptidase activity.
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Whitmania pigra destabilase ortholog (Huang 2026) — isopeptidase + clot-destabilizing activity; C-terminal IPATETTTEI deletion enhances isopeptidase activity.
- Evidence level
- In vitro
- Drug vs leech
- Recombinant (genetically expressed)
- Safety domains
- Bleeding
Clinical translation limit
WpDestabilase's in vitro clot-destabilizing activity does NOT establish clinical efficacy. No FDA-approved derivative exists; W. pigra is a non-hematophagous TCM leech, not the FDA-cleared K040187 species.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 16,300 Da
- Source species
- Whitmania pigra
- Discovered
- 2026 · Huang B et al.
Biological Targets
- → isopeptide ε-(γ-Glu)-Lys bonds in cross-linked fibrin
Key Citations
- Huang B et al. (2026), Protein Expr Purif · PMID 42092413
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.