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Fibrinogen adsorption on biomaterials--a numerical study.

Daniel Siegismund¹, Thomas F Keller, Klaus D Jandt

¹Institute of Materials Science and Technology, Friedrich-Schiller-University Jena, Löbdergraben 32, Jena, Germany. daniel.siegismund@uni-jena.de

Macromolecular Bioscience

|July 6, 2010

Summary

This study presents a new model for protein adsorption on surfaces, simulating fibrinogen behavior. Surface hydrophobicity significantly influences fibrinogen adsorption dynamics, as shown by simulations and atomic force microscopy.

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Area of Science:

Biophysics
Surface Science
Computational Biology

Background:

Protein adsorption on solid surfaces is crucial in biomaterials and biomedical devices.
Understanding non-globular protein behavior, like fibrinogen, presents unique modeling challenges.

Purpose of the Study:

To develop and validate a computational model for fibrinogen adsorption on solid surfaces.
To investigate the impact of surface properties, specifically hydrophobicity, on protein adsorption dynamics.

Main Methods:

Two-dimensional cellular automata simulations were employed to model fibrinogen adsorption.
The model incorporated mass transfer, adsorption kinetics, and surface diffusion of molecules and clusters.
Atomic force microscopy was used to experimentally validate simulation results on silicon surfaces with varying hydrophobicity.

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Main Results:

The model accurately represents key physical processes governing fibrinogen adsorption.
Surface hydrophobicity was identified as a critical factor influencing fibrinogen molecule and cluster behavior.
Simulated adsorption patterns showed good agreement with experimental atomic force microscopy data.

Conclusions:

The developed model provides a robust framework for studying non-globular protein adsorption.
Surface hydrophobicity plays a significant role in dictating the outcome of fibrinogen adsorption.
This research offers insights into protein-surface interactions relevant to biomedical applications.