title: Native protein nanolithography that can write, read and erase.
abstract: The development of systematic approaches to explore protein-protein interactions and dynamic protein networks is at the forefront of biological sciences. Nanopatterned protein arrays offer significant advantages for sensing applications, including short diffusion times, parallel detection of multiple targets and the requirement for only tiny amounts of sample. Atomic force microscopy (AFM) based techniques have successfully demonstrated patterning of molecules, including stable proteins, with submicrometre resolution. Here, we introduce native protein nanolithography for the nanostructured assembly of even fragile proteins or multiprotein complexes under native conditions. Immobilized proteins are detached by a novel vibrational AFM mode (contact oscillation mode) and replaced by other proteins, which are selectively self-assembled from the bulk. This nanolithography permits rapid writing, reading and erasing of protein arrays in a versatile manner. Functional protein complexes may be assembled with uniform orientation at dimensions down to 50 nm. Such fabrication of two-dimensionally arranged nano-objects with biological activity will prove powerful for proteome-wide interaction screens and single molecule/virus/cell analyses.
authors.affiliation: Institute of Biochemistry, Biocenter, Johann Wolfgang Goethe-University, Max-von-Laue-Str. 9, D-60438 Frankfurt, Germany.
authors.forename: Ali
authors.initials: A
authors.lastname: Tinazli
authors.forename: Jacob
authors.initials: J
authors.lastname: Piehler
authors.forename: Mirjam
authors.initials: M
authors.lastname: Beuttler
authors.forename: Reinhard
authors.initials: R
authors.lastname: Guckenberger
authors.forename: Robert
authors.initials: R
authors.lastname: Tampé
mesh_terms: D003460:Crystallization / Q000379:methods*; D016247:Information Storage and Retrieval / Q000379:methods*; D046911:Macromolecular Substances / Q000737:chemistry; D008422:Materials Testing; D008968:Molecular Conformation; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D036103:Nanotechnology / Q000379:methods*; D010316:Particle Size; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D046911:Macromolecular Substances; D011506:Proteins