End-grafted poly(ethylene glycol) (PEG) brushes are widely used in order to suppress undesired protein adsorption to surfaces exposed to blood or other biological fluids. The specific adsorption of antibodies (Abs) to PEG brushes associated with PEG's antigenicity is drawing increasing attention because it can affect clinical applications. Here, the adsorption to PEG brushes of two Ab types, specifically binding the polymer backbone and the polymer endpoints, is structurally characterized by neutron reflectometry. The measurements yield volume fraction profiles of PEG and of the adsorbed Abs with sub-nanometer resolution perpendicular to the surface. For all brush parameters in terms of grafting density and polymerization degree, the Ab profiles clearly differ between backbone binders and endpoint binders. The adsorbed Ab amount per unit area is substantial for both Ab types and for all brush parameters investigated, even for dense brushes, which impose a considerable osmotic barrier to Ab insertion. The results therefore indicate that variation of brush parameters alone is insufficient to prevent undesired Ab adsorption. Instead, our work motivates further efforts in the search for nonantigenic brush chemistry.