Leech Antistasin-Homolog Anticoagulant
Novel Hirudo medicinalis salivary protein (28% identity to antistasin) with stronger aPTT inhibition than hirudin at equimolar concentration — Manuvera 2024.
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Novel Hirudo medicinalis salivary protein (28% identity to antistasin) with stronger aPTT inhibition than hirudin at equimolar concentration — Manuvera 2024.
- Evidence level
- In vitro
- Drug vs leech
- Recombinant (genetically expressed)
- Safety domains
- Bleeding
Clinical translation limit
This new protein's in vitro aPTT activity at equimolar superior to hirudin does NOT establish clinical efficacy. No FDA-approved derivative exists; mechanistic discrepancy between clotting-positive and chromogenic-negative FXa assays requires further investigation.
Molecular Profile
- Category
- Anticoagulant
- Evidence tier
- Preclinical
- Molecular weight
- 15,000 Da
- Source species
- Hirudo medicinalis
- Discovered
- 2024 · Manuvera VA et al.
Biological Targets
- → thrombin (direct, weaker than hirudin)
- → factor Xa-related clotting (clotting-assay positive, chromogenic-negative)
Key Citations
- Manuvera VA et al. (2024), Biochem Biophys Res Commun · PMID 38241814
External Resources
Related Anticoagulant Compounds
Hirudin
The most potent natural thrombin inhibitor — and the molecular template for three FDA-approved direct thrombin inhibitor drugs.
Antistasin
Factor Xa inhibitor — prototype molecule that inspired the entire DOAC drug class (rivaroxaban, apixaban).
Ghilanten
Factor Xa inhibitor with anti-metastatic activity in animal cancer models — translational dual-use compound.
Lefaxin
Factor Xa inhibitor with anti-inflammatory properties.