Attachment of proteins to molecular printboards through orthogonal multivalent linkers.
The attachment of proteins to a surface in such a way that the protein remains functional, is a key issue in many biotechnological processes. Here, we describe the controlled attachment with respect to kinetics, thermodynamics and orientation of SAv (streptavidin) through an orthogonal linker to beta-cyclodextrin selfassembled monolayers. Both a univalent and a bivalent linker are used for this process. The immobilization strategy with the bivalent linker allows the stepwise adsorption of SAv on to the surface, allowing heterofunctionalization of SAv and thus the build-up of more complex bionanostructures at the surface.
Ludden
M J W
MJ
Laboratory of Molecular Nanofabrication, MESA+ Institute for Nanotechnology, University of Twente, PO Box 217, 7500 AE Enschede, The Netherlands.
Huskens
J
J
D000327:Adsorption; D001672:Biocompatible Materials / Q000737:chemistry*; D001709:Biotechnology; D020099:Coated Materials, Biocompatible / Q000737:chemistry; D007700:Kinetics; D008422:Materials Testing; D018625:Microscopy, Atomic Force; D046912:Multiprotein Complexes; D049329:Nanostructures / Q000737:chemistry; D036103:Nanotechnology; D011506:Proteins / Q000737:chemistry*; D019809:Streptavidin / Q000737:chemistry; D013816:Thermodynamics; D047392:beta-Cyclodextrins / Q000737:chemistry
D001672:Biocompatible Materials; D020099:Coated Materials, Biocompatible; D046912:Multiprotein Complexes; D011506:Proteins; D047392:beta-Cyclodextrins; D019809:Streptavidin; C031215:betadex