Sociedad Americana de Hirudoterapia

Therostasin

Factor Xa inhibitor from Theromyzon tessulatum — Kunitz-domain analog with novel selectivity profile.

Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Therostasin compared with other characterized leech-derived compoundsHementerin80 kDaHementin80 kDaHementin-Like Protein (HLP-1)80 kDaLeech Collagenase70 kDaHaemadipsa yanyuanensis Progr…70 kDaLeech Apyrase67 kDaCalin65 kDaHyaluronidase60 kDaAntithrombin III binding prot…58 kDaCollagenolytic Fibrinolysin55 kDaLeech Thrombospondin-Like Pro…50 kDaTherostasin14 kDa
Molecular weight (kilodaltons) of Therostasin (highlighted) alongside other characterized leech salivary compounds. Smaller proteins/peptides generally diffuse and act faster.

Mechanistic Evidence Box

Preclinical / mechanistic
Page type
Compound profile
Evidence type
Factor Xa inhibitor from Theromyzon tessulatum — Kunitz-domain analog with novel selectivity profile.
Evidence level
In vitro
Drug vs leech
Purified natural compound
Safety domains
Bleeding

Clinical translation limit

Therostasin's in vitro inhibition of Factor Xa does not establish clinical efficacy. No FDA-approved derivative exists. Mechanism is preclinical/biochemical only.

Molecular Profile

Category
Anticoagulant
Evidence tier
Preclinical
Molecular weight
14,000 Da
Source species
Theromyzon tessulatum
Discovered
1999 · Chopin V et al.
Therostasin molecular structure

Biological Targets

  • Factor Xa

Key Citations

  1. Chopin V et al. (2000), J Biol Chem · PMID 10852926

External Resources

    Related Anticoagulant Compounds

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