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Updated: Jun 2, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Mechanisms of fibrinogen adsorption at solid substrates
Zbigniew Adamczyk1, Jakub Barbasz, Michał Cieśla
1J. Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, 30-239 Kraków, Niezapominajek 8, Poland. ncadamcz@cyf-kr.edu.pl
This study models fibrinogen adsorption using random sequential adsorption (RSA), revealing distinct irreversible and reversible binding layers. The research quantifies maximum surface concentrations and adsorption energies, aiding in understanding protein interactions on surfaces.
Area of Science:
- Biophysics
- Surface Science
- Physical Chemistry
Background:
- Fibrinogen adsorption is crucial for biomaterial interactions and thrombosis.
- Understanding protein adsorption mechanisms on surfaces is essential for biomedical applications.
- Existing models often simplify protein structure and adsorption dynamics.
Purpose of the Study:
- To theoretically investigate fibrinogen adsorption using the random sequential adsorption (RSA) model.
- To differentiate and quantify irreversible (side-on) and reversible (end-on) fibrinogen adsorption.
- To predict adsorption isotherms, kinetics, and binding energies for fibrinogen.
Main Methods:
- Utilized the random sequential adsorption (RSA) model to simulate fibrinogen adsorption.
- Modeled fibrinogen as a linear chain of beads of varying sizes.
- Calculated maximum surface concentrations for both irreversible and reversible adsorption layers.
- Determined the surface blocking function (ASF) for end-on adsorption.
- Predicted adsorption isotherms and kinetics under diffusion and convection.
- Interpreted experimental data from TIRF and ellipsometry.
Main Results:
- Maximum surface concentration for the end-on (reversible) monolayer is 6.13 × 10^3 μm⁻².
- Maximum surface concentration for the side-on (irreversible) monolayer is 2.27 × 10^3 μm⁻².
- Total maximum surface concentration for both orientations is 8.40 × 10^3 μm⁻².
- Equilibrium adsorption constant for end-on adsorption is 8.04 × 10⁻³ m.
- Predicted adsorption energy minimum of -17.4 kT (ΔG = -41.8 kJ mol⁻¹).
Conclusions:
- The RSA model successfully predicts fibrinogen adsorption behavior, including distinct reversible and irreversible binding.
- Theoretical predictions align with experimental data, validating the model's accuracy.
- The study provides insights into anisotropic protein adsorption mechanisms on heterogeneous surfaces.
- Findings contribute to understanding protein-surface interactions for biomaterial design and diagnostics.
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