Tandem-Hirudin (TH)
Bivalent tandem-domain hirudin homolog from Hirudinaria manillensis — two globular domains without C-terminal tail; structurally distinct from kissing-bug / tick analogs (Lukas 2022).
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Bivalent tandem-domain hirudin homolog from Hirudinaria manillensis — two globular domains without C-terminal tail; structurally distinct from kissing-bug / tick analogs (Lukas 2022).
- Evidence level
- In vitro
- Drug vs leech
- Recombinant (genetically expressed)
- Safety domains
- Bleeding
Clinical translation limit
Tandem-Hirudin's structural homology to hirudin does NOT establish functional thrombin inhibition or clinical efficacy. Lukas 2022 in vitro assays showed NO thrombin-inhibitory potency; functional role and physiological target remain uncharacterized.
Molecular Profile
- Category
- Anticoagulant
- Evidence tier
- Preclinical
- Molecular weight
- 14,000 Da
- Source species
- Hirudinaria manillensis
- Discovered
- 2022 · Lukas P et al.
Biological Targets
- → thrombin (structural homolog; functional activity equivocal)
Key Citations
- Lukas P et al. (2022), Parasitol Res · PMID 36006484
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.