HmDestabilase
Hirudinaria manillensis destabilase / i-type lysozyme (Gao 2025) — isopeptidase + lysozyme activity, salivary-gland-upregulated on blood feeding.
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Hirudinaria manillensis destabilase / i-type lysozyme (Gao 2025) — isopeptidase + lysozyme activity, salivary-gland-upregulated on blood feeding.
- Evidence level
- In vitro
- Drug vs leech
- Recombinant (genetically expressed)
- Safety domains
- Bleeding
Clinical translation limit
HmDestabilase's in vitro isopeptidase / lysozyme activity does NOT establish clinical efficacy. No FDA-approved derivative exists; H. manillensis is not the FDA-cleared K040187 medicinal leech species.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 16,000 Da
- Source species
- Hirudinaria manillensis
- Discovered
- 2025 · Gao T et al.
Biological Targets
- → isopeptide bonds in fibrin
- → bacterial peptidoglycan (lysozyme activity)
Key Citations
- Gao T et al. (2025), Protein Expr Purif · PMID 40107525
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.