American Society of Hirudotherapy

Surface modification with PEG and hirudin for protein resistance and thrombin neutralization in blood contact

In vitro experimental study published in Colloids and surfaces. B, Biointerfaces (2010)

Last Updated: November 1, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewDrug DevelopmentGenomics & ProteomicsAlibeik S, Zhu S, Brash J · Colloids and surfaces. B, Biointerfaces, 2010

Abstract

In this work, we hypothesize that a surface modified with both polyethylene glycol (PEG) and hirudin may provide a non-fouling, thrombin-neutralizing surface suitable for blood contacting applications. With gold as a model substrate we used two different approaches to the preparation of such a surface: (1) a "direct" method in which PEG was conjugated to hirudin and the conjugate was then immobilized on the gold; (2) a "sequential" method in which PEG was immobilized on the gold and hirudin then attached to the immobilized PEG. The surfaces were characterized by water contact angle, ellipsometry and XPS. The biological properties were investigated by measuring protein adsorption (fibrinogen and thrombin) from buffer and plasma; thrombin inhibition was measured using a chromogenic substrate assay. Hirudin immobilization was found to be more efficient on surfaces prepared by the "direct" method. "Sequential" surfaces, however, despite having a lower density of hirudin, showed greater biological activity (thrombin binding and inhibition).

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'tReview
Indexed MeSH termsAdsorptionFibrinogenGoldHirudinsHumansSurface PropertiesThrombin

Summary

Using gold as a model blood-contacting substrate, the authors compared direct and sequential PEG-hirudin immobilization; the direct method bound more hirudin, but lower-density sequential surfaces showed greater thrombin binding by adsorption assay and greater thrombin inhibition by chromogenic assay.

Context

This study examined whether gold surfaces co-modified with polyethylene glycol (PEG) and hirudin could resist protein adsorption and neutralize thrombin for potential blood-contacting biomaterial applications, comparing two immobilization strategies. The work characterizes hirudin's thrombin-inhibiting activity in a surface-engineered context, which is mechanistically related to anticoagulation and blood compatibility. However, the abstract describes hirudin solely as an immobilized reagent with no leech, salivary, or hirudotherapy context whatsoever. The study is limited to in-vitro surface characterization and protein-adsorption assays on model gold substrates, with no clinical testing or therapeutic application demonstrated.

Citation

Reference (Vancouver style)

Alibeik S, Zhu S, Brash JL. Surface modification with PEG and hirudin for protein resistance and thrombin neutralization in blood contact. Colloids Surf B Biointerfaces. 2010;81(2):389-396. doi:10.1016/j.colsurfb.2010.07.024. PMID: 20709502

Bibliographic details (authors, volume, pages, DOI) are taken from the PubMed record.

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