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Related Experiment Videos

Time-dependent conformational changes in fibrinogen measured by atomic force microscopy.

Aashiish Agnihotri1, Christopher A Siedlecki

  • 1Department of Bioengineering, Pennsylvania State University, College of Medicine, Biomedical Engineering Institute, Hershey 17033, USA.

Langmuir : the ACS Journal of Surfaces and Colloids
|September 24, 2004
PubMed
Summary

Atomic force microscopy revealed how fibrinogen protein structure changes upon adsorption to surfaces. Fibrinogen spreads differently on hydrophobic graphite versus hydrophilic mica, indicating surface properties influence protein behavior.

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Area of Science:

  • Biophysics
  • Surface Science
  • Protein Chemistry

Background:

  • Fibrinogen is a key protein in blood coagulation.
  • Understanding protein adsorption is crucial for biomaterial design and diagnostics.
  • Surface properties significantly influence protein structure and function.

Purpose of the Study:

  • To investigate the time-dependent structural changes of fibrinogen adsorbed on hydrophobic graphite and hydrophilic mica surfaces.
  • To determine the kinetics and thermodynamics of fibrinogen spreading on different model surfaces.
  • To elucidate the role of surface hydrophobicity in protein-surface interactions.

Main Methods:

  • Tapping-mode atomic force microscopy (AFM) was employed to image fibrinogen structure.
  • Adsorption studies were conducted under aqueous conditions on graphite and mica.

Related Experiment Videos

  • Height measurements of fibrinogen domains over time were analyzed using kinetic models.

    • Main Results:

    • Fibrinogen adopted a characteristic trinodular form upon adsorption.
    • Four distinct orientation states were observed, varying with surface type and time.
    • On graphite, fibrinogen height decreased over time, suggesting unfolding and spreading.
    • On mica, fibrinogen height increased, indicating a different adsorption mechanism.
    • Stronger adhesion was observed on hydrophobic graphite compared to hydrophilic mica.

    Conclusions:

    • Surface hydrophobicity dictates fibrinogen's adsorption behavior and structural rearrangements.
    • A two-step spreading model is proposed to explain initial fibrinogen adsorption on hydrophobic surfaces.
    • AFM provides valuable insights into protein-surface interactions relevant to biomaterials and biological processes.