title: Multifunctional clickable and protein-repellent magnetic silica nanoparticles.
abstract: Silica nanoparticles are versatile materials whose physicochemical surface properties can be precisely adjusted. Because it is possible to combine several functionalities in a single carrier, silica-based materials are excellent candidates for biomedical applications. However, the functionality of the nanoparticles can get lost upon exposure to biological media due to uncontrolled biomolecule adsorption. Therefore, it is important to develop strategies that reduce non-specific protein-particle interactions without losing the introduced surface functionality. Herein, organosilane chemistry is employed to produce magnetic silica nanoparticles bearing differing amounts of amino and alkene functional groups on their surface as orthogonally addressable chemical functionalities. Simultaneously, a short-chain zwitterion is added to decrease the non-specific adsorption of biomolecules on the nanoparticles surface. The multifunctional particles display reduced protein adsorption after incubation in undiluted fetal bovine serum as well as in single protein solutions (serum albumin and lysozyme). Besides, the particles retain their capacity to selectively react with biomolecules. Thus, they can be covalently bio-functionalized with an antibody by means of orthogonal click reactions. These features make the described multifunctional silica nanoparticles a promising system for the study of surface interactions with biomolecules, targeting, and bio-sensing.
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
authors.forename: Diego
authors.initials: D
authors.lastname: Estupiñán
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
authors.forename: Markus B
authors.initials: MB
authors.lastname: Bannwarth
authors.affiliation: Lafayette College, Department of Chemistry, Easton, PA 18042, USA.
authors.forename: Steven E
authors.initials: SE
authors.lastname: Mylon
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
authors.forename: Katharina
authors.initials: K
authors.lastname: Landfester
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany and Institute of Materials Science (ICMUV), University of Valencia, PO Box 22085, 46071 Valencia, Spain. rafael.munoz@uv.es.
authors.forename: Rafael
authors.initials: R
authors.lastname: Muñoz-Espí
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany and Vidyasirimedhi Institute of Science and Technology (VISTEC), School of Molecular Science and Engineering, Department of Material Science and Engineering, Rayong, Thailand. crespy@mpip-mainz.mpg.de.
authors.forename: Daniel
authors.initials: D
authors.lastname: Crespy
mesh_terms: D000327:Adsorption; D000818:Animals; D002417:Cattle; D000067493:Dynamic Light Scattering; D004591:Electrophoresis, Polyacrylamide Gel; D052203:Ferrosoferric Oxide / Q000737:chemistry; D008280:Magnetics; D009113:Muramidase / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D011137:Polystyrenes / Q000737:chemistry; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*; D013499:Surface Properties; D013818:Thermogravimetry
chemical_list: D011137:Polystyrenes; D012710:Serum Albumin, Bovine; D012822:Silicon Dioxide; D009113:Muramidase; D052203:Ferrosoferric Oxide