Sociedad Americana de Hirudoterapia

Leech Metalloprotease Inhibitor

TIMP / netrin-domain metalloprotease inhibitor variant in leech salivary transcriptome — putative MMP regulator at bite site.

Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Leech Metalloprotease 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 Metalloprotease Inhibit…22 kDa
Molecular weight (kilodaltons) of Leech Metalloprotease 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
TIMP / netrin-domain metalloprotease inhibitor variant in leech salivary transcriptome — putative MMP regulator at bite site.
Evidence level
In vitro
Drug vs leech
Purified natural compound

Clinical translation limit

Predicted metalloprotease-inhibitor activity does NOT establish clinical efficacy. No FDA-approved derivative exists.

Molecular Profile

Category
Proteinase Inhibitor
Evidence tier
Preclinical
Molecular weight
22,000 Da
Source species
Hirudo medicinalis
Discovered
2018
Leech Metalloprotease Inhibitor molecular structure

Biological Targets

  • matrix metalloproteinases (MMP-2 / MMP-9 predicted)

External Resources

    Related Proteinase Inhibitor Compounds

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