Sociedad Americana de Hirudoterapia

Poeciguamerin

Antistasin-domain dual analgesic + antithrombotic serine protease inhibitor from Poecilobdella manillensis — Wang 2023 explains the painless-bleed phenotype.

Preclínico / mecanísticoLast updated: 2026-05-27 · Reviewed by ASH Editorial Board
Molecular weight of Poeciguamerin 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 kDaPoeciguamerin5.5 kDa
Molecular weight (kilodaltons) of Poeciguamerin (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
Antistasin-domain dual analgesic + antithrombotic serine protease inhibitor from Poecilobdella manillensis — Wang 2023 explains the painless-bleed phenotype.
Evidence level
Preclinical (animal)
Drug vs leech
Purified natural compound
Safety domains
Bleeding

Clinical translation limit

Poeciguamerin's preclinical analgesic + antithrombotic activity in murine models does NOT establish clinical efficacy in humans. No FDA-approved derivative exists; P. manillensis is not the FDA-cleared K040187 medicinal leech species.

Molecular Profile

Category
Proteinase Inhibitor
Evidence tier
Preclinical
Molecular weight
5,500 Da
Source species
Poecilobdella manillensis
Discovered
2023 · Wang C et al.
Poeciguamerin molecular structure

Biological Targets

  • leukocyte elastase (primary)
  • FXIIa
  • kallikrein

Key Citations

  1. Wang C et al. (2023), Int J Mol Sci · PMID 37446275

External Resources

    Related Proteinase Inhibitor Compounds

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