American Society of Hirudotherapy

Effect of O-glycosylation and tyrosine sulfation of leech-derived peptides on binding and inhibitory activity against thrombin

Basic science published in Chem Commun (2011)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Research reportDrug DevelopmentSalivary PharmacologyHsieh YS et al. · Chemical communications, 2011

Abstract

Synthesis of sulfated and unsulfated (glyco)peptide fragments of Hirudin P6 (a potent anticoagulant from the leech Hirudinaria manillensis) is described. The effect of O-glycosylation and tyrosine sulfation on thrombin binding and peptidolytic activity was investigated, together with the inhibition of fibrinogen cleavage.

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

Publication typeJournal ArticleResearch Support, Non-U.S. Gov't
Indexed MeSH termsBinding SitesGlycosylationMolecular ConformationPeptidesStructure-Activity RelationshipThrombinTyrosine

Summary

Synthesized sulfated and glycosylated Hirudin P6 fragment peptides show tyrosine sulfation enhances thrombin binding.

Why This Matters for Hirudotherapy

This study synthesized sulfated and unsulfated (glyco)peptide fragments of Hirudin P6—a potent anticoagulant from the leech Hirudinaria manillensis—and examined the effect of O-glycosylation and tyrosine sulfation on thrombin binding, peptidolytic activity, and inhibition of fibrinogen cleavage. This is relevant to ASH because it clarifies structure–activity relationships of a leech-derived thrombin inhibitor, informing how post-translational modifications modulate anticoagulant potency. The caveat is that this is an in-vitro biochemical/synthetic peptide study with no whole leech, no secretome, and no clinical or animal data, so relevance to actual hirudotherapy is indirect and mechanistic only.

Citation

Effect of O-glycosylation and tyrosine sulfation of leech-derived peptides on binding and inhibitory activity against thrombin.

Hsieh YS et al. · Chemical communications, 2011

DOI

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

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