Molecular Organization of Proteins in Nano-Dimensions

Robert Tampé

Institute of Biochemistry, Biocenter, Johann-Wolfgang-Goethe-University, Marie-Curie-Str. 9, D-60439 Frankfurt/Main, Germany




Due to their self-organizing and dynamic properties, biomaterials such as lipids and peptides produce a wide spectrum of functionality. These nanobionic scaffolds are ideal to organize and manipulate proteins in two dimensions on nanoscale. The expression of fusion histidine fusion proteins, which specifically interact with metal-chelating complexes, is a well-established technique of the purification and characterization of gene products. We have combined this approach with the properties of self-organizing systems by the synthesis of metal-chelating lipids, thiols and polypeptides. Proteins can be specifically immobilized and highly oriented at these functionalized interfaces, eventually leading to protein arrays or even two-dimensional protein crystals. These protein arrays are of central interest e.g. for catalytic, switching and sensing (nano)devices. Alternatively, metal-chelating amino acids as non-natural building block in polypeptides are used for a rational design of synthetic receptors, the control of protein-protein interaction or even switchable protein function.