title: Quantitative evaluation of interaction force between functional groups in protein and polymer brush surfaces.
abstract: To understand interactions between polymer surfaces and different functional groups in proteins, interaction forces were quantitatively evaluated by force-versus-distance curve measurements using atomic force microscopy with a functional-group-functionalized cantilever. Various polymer brush surfaces were systematically prepared by surface-initiated atom transfer radical polymerization as well-defined model surfaces to understand protein adsorption behavior. The polymer brush layers consisted of phosphorylcholine groups (zwitterionic/hydrophilic), trimethylammonium groups (cationic/hydrophilic), sulfonate groups (anionic/hydrophilic), hydroxyl groups (nonionic/hydrophilic), and n-butyl groups (nonionic/hydrophobic) in their side chains. The interaction forces between these polymer brush surfaces and different functional groups (carboxyl groups, amino groups, and methyl groups, which are typical functional groups existing in proteins) were quantitatively evaluated by force-versus-distance curve measurements using atomic force microscopy with a functional-group-functionalized cantilever. Furthermore, the amount of adsorbed protein on the polymer brush surfaces was quantified by surface plasmon resonance using albumin with a negative net charge and lysozyme with a positive net charge under physiological conditions. The amount of proteins adsorbed on the polymer brush surfaces corresponded to the interaction forces generated between the functional groups on the cantilever and the polymer brush surfaces. The weakest interaction force and least amount of protein adsorbed were observed in the case of the polymer brush surface with phosphorylcholine groups in the side chain. On the other hand, positive and negative surfaces generated strong forces against the oppositely charged functional groups. In addition, they showed significant adsorption with albumin and lysozyme, respectively. These results indicated that the interaction force at the functional group level might be a suitable parameter for understanding protein adsorption.
authors.affiliation: Department of Materials Engineering, ‡Department of Bioengineering, School of Engineering, The University of Tokyo , 7-3-1, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
authors.forename: Sho
authors.initials: S
authors.lastname: Sakata
authors.forename: Yuuki
authors.initials: Y
authors.lastname: Inoue
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Ishihara
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D011108:Polymers / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D011108:Polymers; D011506:Proteins