title: Elastic Properties of Protein Functionalized Nanoporous Polymer Films.
abstract: Retaining the conformational structure and bioactivity of immobilized proteins is important for biosensor designs and drug delivery systems. Confined environments often lead to changes in conformation and functions of proteins. In this study, lysozyme is chemically tethered into nanopores of polystyrene thin films, and submicron pores in poly(methyl methacrylate) films are functionalized with streptavidin. Nanoindentation experiments show that stiffness of streptavidin increases with decreasing submicron pore sizes. Lysozymes in polystyrene nanopores are found to behave stiffer than the submicron pore sizes and still retain their specific bioactivity relative to the proteins on flat surfaces. Our results show that protein functionalized ordered nanoporous polystyrene/poly(methyl methacrylate) films present heterogeneous elasticity and can be used to study interactions between free proteins and designed surfaces.
authors.affiliation: Department of Chemical Engineering and Materials Science, Stevens Institute of Technology , 1 Castle Point on Hudson, Hoboken, New Jersey 07030, United States.
authors.forename: Haoyu
authors.initials: H
authors.lastname: Wang
authors.affiliation: Center for Functional Nanomaterials, Brookhaven National Laboratory , Upton, New York 11973, United States.
authors.forename: Charles T
authors.initials: CT
authors.lastname: Black
authors.affiliation: Department of Chemical Engineering and Materials Science, Stevens Institute of Technology , 1 Castle Point on Hudson, Hoboken, New Jersey 07030, United States.
authors.forename: Pinar
authors.initials: P
authors.lastname: Akcora
mesh_terms: D008567:Membranes, Artificial; D009113:Muramidase / Q000737:chemistry; D058608:Nanopores; D011108:Polymers / Q000737:chemistry*; D011137:Polystyrenes / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*
chemical_list: D008567:Membranes, Artificial; D011108:Polymers; D011137:Polystyrenes; D011506:Proteins; D009113:Muramidase