Sociedad Americana de Hirudoterapia

Leech Pancreatic-Type Trypsin Inhibitor

Leech homolog of pancreatic (Kunitz-type) trypsin inhibitor — broad serine protease inhibition.

Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Leech Pancreatic-Type Trypsin Inhibitor 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 kDaLeech Pancreatic-Type Trypsin…6.5 kDa
Molecular weight (kilodaltons) of Leech Pancreatic-Type Trypsin Inhibitor (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
Leech homolog of pancreatic (Kunitz-type) trypsin inhibitor — broad serine protease inhibition.
Evidence level
In vitro
Drug vs leech
Purified natural compound

Clinical translation limit

Leech pancreatic-type trypsin inhibitor is documented mechanistically only; no human evidence. In vitro inhibition of serine proteases does NOT establish clinical efficacy, and no FDA-approved derivative from this leech homolog exists.

Molecular Profile

Category
Proteinase Inhibitor
Evidence tier
Preclinical
Molecular weight
6,500 Da
Source species
Hirudo medicinalis
Discovered
2011
Leech Pancreatic-Type Trypsin Inhibitor molecular structure

Biological Targets

  • trypsin
  • chymotrypsin
  • plasmin

Key Citations

  1. Liu Z et al. (2019), Parasit Vectors

External Resources

    Related Proteinase Inhibitor Compounds

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