Sociedad Americana de Hirudoterapia

Decorsin

RGD-containing peptide inhibiting platelet GP IIb/IIIa receptor — eptifibatide ancestor.

Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Decorsin 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 kDaDecorsin4.4 kDa
Molecular weight (kilodaltons) of Decorsin (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
RGD-containing peptide inhibiting platelet GP IIb/IIIa receptor — eptifibatide ancestor.
Evidence level
In vitro
Drug vs leech
Purified natural compound
Safety domains
Bleeding

Clinical translation limit

Decorsin itself is NOT an FDA-approved drug. The synthetic peptidomimetic eptifibatide draws partial structural inspiration from decorsin and snake-venom disintegrins, but is a chemically distinct compound with its own clinical evidence base. Decorsin's preclinical mechanism does NOT establish clinical efficacy of whole-leech therapy.

Molecular Profile

Category
Antiplatelet
Evidence tier
Tier A — FDA-approved derivative
Molecular weight
4,400 Da
Source species
Macrobdella decora (North American leech)
Discovered
1990 · Seymour et al.
Derived FDA-approved drug
Conceptual ancestor: eptifibatide (Integrilin)
Decorsin molecular structure

Biological Targets

  • platelet integrin αIIbβ3 (GP IIb/IIIa)

Key Citations

  1. Seymour JL et al. (1990), J Biol Chem

External Resources

    Related Antiplatelet Compounds

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