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Neutron reflectometry from poly (ethylene-glycol) brushes binding anti-PEG antibodies: Evidence of ternary adsorption

Year: 2015

Journal: BIOMATERIALS, Vol. 46, p 95-104, 20170208

Authors: Schneck, Emanuel; Berts, Ida; Halperin, Avraham; Daillant, Jean; Fragneto, Giovanna

Organizations: Inst Laue Langevin, F-38000 Grenoble, France; Max Planck Inst Colloids & Interfaces, Biomat Dept, D-14476 Potsdam, Germany; Univ Munich, Fac Phys, D-80539 Munich, Germany; Univ Munich, CeNS, D-80539 Munich, Germany; Univ Grenoble 1, CNRS, Lab Interdisciplinaire Phys, UMR 5588, F-38042 St Martin Dheres, France; Synchrotron Soleil LOrme Merisiers, F-91192 Gif Sur Yvette, France

Neutron reflectometry provides evidence of ternary protein adsorption within polyethylene glycol (PEG) brushes. Anti-PEG Immunoglobulin G antibodies (Abs) binding the methoxy terminated PEG chain segment specifically adsorb onto PEG brushes grafted to lipid monolayers on a solid support. The Abs adsorb at the outer edge of the brush. The thickness and density of the adsorbed Ab layer, as well as its distance from the grafting surface grow with increasing brush density. At high densities most of the protein is excluded from the brush. The results are consistent with an inverted 'Y' configuration with the two F-AB segments facing the brush. They suggest that increasing the grafting density favors narrowing of the angle between the F-AB segments as well as overall orientation of the bound Abs perpendicular to the surface. (C) 2015 Elsevier Ltd. All rights reserved.