American Society of Hirudotherapy

Multi-target anticoagulant regulation by peptides from medicinal leeches: a unique natural strategy

Review published in Pharm Res (2025)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewDrug DevelopmentSalivary PharmacologyGenomics & ProteomicsShi et al. · Pharmaceutical research, 2025

Abstract

BACKGROUND: Thrombotic diseases remain a major global health burden. Current anticoagulants are often limited by bleeding risks and narrow therapeutic windows, largely due to their single-target mechanisms. In contrast, medicinal leeches secrete diverse peptides that naturally and synergistically modulate multiple steps of the hemostatic system. METHODS: This paper systematically reviews published biochemical, structural, functional, and omics studies on leech-derived anticoagulant peptides, classifying them according to their molecular targets and antithrombotic mechanisms. RESULTS: Leech-derived peptides act synergistically at multiple key points of the coagulation cascade: (1) they inhibit platelet adhesion and aggregation by blocking the vWF-collagen interaction or suppressing GPIIb/IIIa; (2) they directly inhibit core coagulation proteases, such as thrombin and factor Xa; and (3) they interfere with fibrin stabilization and promote its dissolution by inhibiting factor XIIIa or modulating the fibrinolytic and intrinsic protease systems. From a molecular perspective, multispecies omics analyses have revealed a significant expansion of antithrombotic gene families and identified numerous novel peptide candidate genes. CONCLUSIONS: Leech-derived peptides provide a unique natural platform for multi-target anticoagulation and represent promising leads for next-generation antithrombotic agents. Combining traditional purification with genomics-guided discovery will accelerate mechanism elucidation, structural optimization, and translational development.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Publication typeJournal ArticleReview
Indexed MeSH termsAnimalsAnticoagulantsLeechesPeptidesHumansThrombosisBlood CoagulationFibrinolytic Agents

Summary

Review of multi-target anticoagulant regulation by leech-derived peptides as a unique natural strategy with drug-development implications.

Why This Matters for Hirudotherapy

This review systematically examines published biochemical, structural, functional, and omics studies on anticoagulant peptides derived from medicinal leeches, classifying them by molecular target and antithrombotic mechanism. The authors describe how these peptides act synergistically at multiple points—including platelet adhesion/aggregation inhibition, direct protease inhibition (thrombin, factor Xa), and interference with fibrin stabilization—proposing them as promising leads for next-generation antithrombotic agents. This is directly relevant to ASH's domain, as it synthesizes the molecular basis underlying the leech secretome's anticoagulant properties and highlights genomics-guided discovery of novel peptide candidates. As a review of existing literature, it provides no new primary experimental or clinical data, and the described peptides are characterized as leads rather than clinically validated therapies.

Citation

Multi-target anticoagulant regulation by peptides from medicinal leeches: a unique natural strategy.

Shi et al. · Pharmaceutical research, 2025

Added to ASH library: May 27, 2026 · Site last updated: June 18, 2026

This website provides educational information and does not constitute medical advice, diagnosis, or treatment recommendations. Medicinal leech therapy carries clinically meaningful risks and should be performed only by qualified clinicians under institutionally approved protocols. FDA 510(k) clearance for medicinal leeches is limited to specific indications; investigational and off-label discussions are labeled accordingly. For patient-specific guidance, consult a qualified healthcare provider.