Leech Thrombin-Cleavable Peptide
Substrate-mimetic peptide segment identified in leech salivary transcriptome — putative thrombin substrate / competitive inhibitor variant.
Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Substrate-mimetic peptide segment identified in leech salivary transcriptome — putative thrombin substrate / competitive inhibitor variant.
- Evidence level
- Mechanistic discussion
- Drug vs leech
- Purified natural compound
- Safety domains
- Bleeding
Clinical translation limit
This peptide is identified at sequence level only. Hypothesized thrombin interaction is not biochemically verified. No FDA-approved derivative exists and no clinical efficacy is claimed.
Molecular Profile
- Category
- Anticoagulant
- Evidence tier
- Preclinical
- Molecular weight
- 2,000 Da
- Source species
- Hirudo medicinalis
- Discovered
- 2018
Biological Targets
- → thrombin (Factor IIa) cleavage site mimic
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.