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Surface-dependent fibrinopeptide A accessibility to thrombin.

Carri B Geer1, Ioana A Rus, Susan T Lord

  • 1Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Acta Biomaterialia
|June 2, 2007
PubMed
Summary
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Surface properties significantly impact fibrinogen adsorption and fibrin formation. Negatively charged surfaces reduce fibrinopeptide A accessibility, potentially minimizing thrombosis and improving blood-contacting device biocompatibility.

Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Biophysics

Background:

  • Fibrinogen adsorption and fibrin formation are influenced by substrate surface properties.
  • Understanding surface-dependent mechanisms is crucial for developing biocompatible materials.

Purpose of the Study:

  • To investigate the surface-dependent mechanism of fibrinopeptide A (FpA) release and fibrin formation.
  • To determine how surface properties affect FpA accessibility and susceptibility to thrombin cleavage.

Main Methods:

  • Utilized polyclonal anti-FpA IgG binding and surface plasmon resonance (SPR) to assess FpA accessibility.
  • Examined fibrinogen adsorption on methyl- and carboxyl-terminated self-assembled monolayers (SAMs).

Main Results:

Related Experiment Videos

  • FpA accessibility on adsorbed fibrinogen was significantly influenced by surface properties.
  • Hydrophobic surfaces showed approximately 2.7 times more accessible FpA compared to negatively charged surfaces.
  • Thrombin cleaved 100% of available FpA, indicating FpA release is dependent on initial accessibility.

Conclusions:

  • Negatively charged surfaces impair FpA accessibility, reducing fibrin formation.
  • These findings suggest negatively charged surfaces can minimize surface-induced thrombosis.
  • Potential application in developing more biocompatible blood-contacting devices.