Leech Apyrase
ADP-degrading enzyme — prevents platelet aggregation by hydrolyzing ADP at bite site.
Praeklinisch / mechanistischLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- ADP-degrading enzyme — prevents platelet aggregation by hydrolyzing ADP at bite site.
- Evidence level
- Mechanistic discussion
- Drug vs leech
- Leech-derived crude extract
- Safety domains
- Bleeding
Clinical translation limit
Leech apyrase's ADP-degrading mechanism is described at the bite site only and does not establish clinical antiplatelet efficacy. No FDA-approved derivative exists.
Molecular Profile
- Category
- Antiplatelet
- Evidence tier
- Preclinical
- Molecular weight
- 67,000 Da
- Source species
- Hirudo medicinalis
Biological Targets
- → ADP (adenosine diphosphate)
External Resources
Related Antiplatelet Compounds
Calin
Anti-platelet adhesion protein that blocks von Willebrand factor–collagen binding.
Saratin
Anti-platelet adhesion protein blocking collagen-mediated platelet activation.
Decorsin
RGD-containing peptide inhibiting platelet GP IIb/IIIa receptor — eptifibatide ancestor.
Ornatin
RGD-peptide GP IIb/IIIa antagonist — sister molecule to decorsin from a different leech species.