Fibronectin Adsorption at Solid Surfaces
Control of protein adsorption, which can only follow detailed understanding of the adsorption mechanism, is crucial in modern biology, medicine, and technology. Human fibronectin (Fn) is a large multidomain glycoprotein found in insoluble (functional) form in the extracellular matrix (ECM). The biological role of Fn is to promote cell adhesion and thereby influence cell proliferation, migration, differentiation and growth. ECM fibronectin comprises two mostly identical polypeptide chains. Each chain consists of small domains arranged like beads on a string: the smallest FnI (type 1); sparse FnII (type 2); and the most numerous FnIII (type 3). The detailed 3D structure of the entire Fn protein is not known. Nevertheless, the X-ray structure of domain FnIII9 has been recently solved, thereby providing new opportunities for molecular dynamics studies (MD).
The mechanism of FnIII9 fibronectin domain adsorption at mica (hydrophilic and negatively charged), SiO2 and gold surface models is studied using atomistic, molecular dynamics (MD) simulations. Our main aim is to formulate a detailed description of the adsorption processes including the role of the electrostatic field produced by some of these surfaces, and the extent of conformational changes induced by the surface adsorption and its influence on protein activity. The research provides new insight into recent experimental results and leads the design of further experiments, providing essential data for the future development of functionalized surfaces.
For more information about the project contact Dr Karina Kubiak-Ossowska (email@example.com), ARCHIE-WeSt User Support Officer at the University of Strathclyde or Dr Paul Mulheran, Senior Lecturer at the Department of Chemical and Process Engineering at the University of Strathclyde.
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