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Related Experiment Videos

Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces.

X Sun1, H Sheardown, P Tengvall

  • 1Department of Chemical Engineering, McMaster University, Hamilton, Ontario L8S 4L7, Canada.

Journal of Biomedical Materials Research
|November 24, 1999
PubMed
Summary

Modified gold surfaces with specific peptides effectively capture and inhibit thrombin, a key blood clotting protein. The Cys-(D)Phe-Pro-Arg peptide surface demonstrated superior performance as an antithrombogenic material.

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Biochemistry

Background:

  • Thrombin is a critical enzyme in blood coagulation.
  • Developing materials to control thrombin activity is essential for preventing thrombosis.
  • Peptides related to known thrombin inhibitors can be immobilized on surfaces.

Purpose of the Study:

  • To create and evaluate peptide-modified gold surfaces for thrombin scavenging.
  • To assess the affinity and selectivity of these surfaces for thrombin from buffer and plasma.
  • To determine the antithrombogenic potential of these peptide surfaces.

Main Methods:

  • Chemisorption of N-terminal cysteine peptides onto gold-coated polyurethane films.
  • Confirmation of peptide attachment using water contact angle and X-ray photoelectron spectroscopy.

Related Experiment Videos

  • Assays for thrombin adsorption, activity inhibition, and selectivity from plasma.

    • Main Results:

    • Peptide attachment to gold surfaces was successfully confirmed.
    • The modified surfaces demonstrated high affinity for thrombin adsorption from buffer.
    • The Cys-(D)Phe-Pro-Arg surface showed particularly high thrombin affinity and inhibited thrombin activity.
    • Selective uptake of thrombin from plasma was observed.

    Conclusions:

    • Peptide-modified gold surfaces can effectively scavenge and inhibit thrombin.
    • The Cys-(D)Phe-Pro-Arg surface exhibits promising antithrombogenic properties.
    • These surfaces hold potential for use in antithrombogenic medical devices.