Prof. (apl.) Dr. Reiner Dahint – Biosensors and Biomaterials Research Group
Conformation and Activity of Surface-Bound Biomolecules
Surface-bound biomolecules have gained growing attention in the field of biotechnology and biomedicine. Important examples include heterogeneous immunoassays and biosensors for the specific detection of dissolved antigens, DNA and peptide chips for genome analysis, or the control of cell adsorption onto surfaces by adhesion proteins. Moreover, nonspecifically adsorbed proteins significantly affect the biocompatibility of implants. In order to provide the desired function of biomolecule-derivatized surfaces it is not only crucially important to control the amount and type of adsorbed biomolecules, but also to maintain their native molecular conformation
While proteins adsorbed to homogeneous surfaces tend to unfold and lose their original functionality, it may be expected that their conformation and activity can be stabilized on structured surfaces, where the proteins are confined to nanoscale adsorption sites. Thus, the goal of our studies is to precisely control the conformation and maintain the activity of surface-bound biomolecules by an appropriate choice of the geometry and surface chemistry of the adsorption sites and their environment. Moreover, successively increasing the size of appropriately derivatized adsorption sites may lead to partial unfolding of the proteins resulting in partial loss of function. One may speculate that this concept will facilitate the fabrication of surfaces with tunable biological function, providing new options in the deliberate design of biofunctional surfaces.