Sociedad Americana de Hirudoterapia

Hirudo tianjinensis Multimeric Hirudin

Multi-domain hirudin superfamily proteins from H. tianjinensis (Kalatehjari 2026) — two-or-more central globular domains per molecule.

Preclínico / mecanísticoLast updated: 2026-05-27 · Reviewed by ASH Editorial Board
Molecular weight of Hirudo tianjinensis Multimeric Hirudin 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 kDaHirudo tianjinensis Multimeri…15 kDa
Molecular weight (kilodaltons) of Hirudo tianjinensis Multimeric Hirudin (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
Multi-domain hirudin superfamily proteins from H. tianjinensis (Kalatehjari 2026) — two-or-more central globular domains per molecule.
Evidence level
In vitro
Drug vs leech
Recombinant (genetically expressed)
Safety domains
Bleeding

Clinical translation limit

Multimeric hirudin's in vitro thrombin inhibition does NOT establish clinical efficacy. No FDA-approved multimeric hirudin derivative exists; clinical hirudin analogs (lepirudin, desirudin) are monomeric.

Molecular Profile

Category
Anticoagulant
Evidence tier
Preclinical
Molecular weight
15,000 Da
Source species
Hirudo tianjinensis
Discovered
2026 · Kalatehjari P et al.
Hirudo tianjinensis Multimeric Hirudin molecular structure

Biological Targets

  • thrombin (multivalent binding via multiple globular domains)

Key Citations

  1. Kalatehjari P et al. (2026), Parasitol Res · PMID 41653280

External Resources

    Related Anticoagulant Compounds

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