Sociedad Americana de Hirudoterapia

Hementin-Like Protein (HLP-1)

Fibrinogenolytic / anti-platelet protein homologous to hementin — disrupts platelet aggregation.

Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Hementin-Like Protein (HLP-1) compared with other characterized leech-derived compoundsHementin-Like Protein (HLP-1)80 kDaHementerin80 kDaHementin80 kDaLeech Collagenase70 kDaHaemadipsa yanyuanensis Progr…70 kDaLeech Apyrase67 kDaCalin65 kDaHyaluronidase60 kDaAntithrombin III binding prot…58 kDaCollagenolytic Fibrinolysin55 kDaLeech Thrombospondin-Like Pro…50 kDaLHyal (Leech Hyaluronidase)50 kDa
Molecular weight (kilodaltons) of Hementin-Like Protein (HLP-1) (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
Fibrinogenolytic / anti-platelet protein homologous to hementin — disrupts platelet aggregation.
Evidence level
In vitro
Drug vs leech
Purified natural compound
Safety domains
Bleeding

Clinical translation limit

HLP-1 is documented mechanistically only; no human evidence. Homology to hementin does NOT establish clinical efficacy, and no FDA-approved derivative exists.

Molecular Profile

Category
Antiplatelet
Evidence tier
Preclinical
Molecular weight
80,000 Da
Source species
Haementeria-related species
Discovered
2006
Hementin-Like Protein (HLP-1) molecular structure

Biological Targets

  • fibrinogen
  • platelet aggregation

External Resources

    Related Antiplatelet Compounds

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