Group leader: Uno Carlsson
Proteins at interfaces have captured the attention of much research during the last few decades and are of increasing interest because of the implications in a wide variety of fields .
Little is known about the direction and specificity of protein adsorption to solid surfaces, a knowledge that is of great importance in many biotechnological applications. In order to resolve in what direction a protein, with known structure and surface potentials, binds to silica nanoparticles, fluorescent probes were attached to different areas on the surface of the enzyme HCA II. Interestingly, by this approach it was clearly demonstrated that the adsorption of the native protein is specific to limited regions at the surface of the N-terminal domain of the protein. Clearly the adsorption is directed by positively charged areas on the protein surface towards the negatively charged silica surface at conditions, low pH, when specific binding occurs ( Karlsson M., U. Carlsson (2005) Biophys. J. 88, 3536-3544; Karlsson, M., U. Carlsson (2007) Encyclopedia of Surface and Colloidal Science 2nd edition 1, 1-16 ).
A continuation of this work is now in progress where we are attempting to reorient the adsorption direction of the protein. The strategy is by protein engineering to change the surface charge of the protein in specific regions to be able to direct the adsorption.
To conclude it is warranted in many biotechnological applications to be able to direct the adsorbed protein in a way that allows binding of ligands, substrates, protein partners etc in order to retain an efficient biological function.
Responsible for this page: Maria Sunnerhagen
Last updated: 05/27/08