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End Point Versus Backbone Specificity Governs Characteristics of Antibody Binding to Poly(ethylene glycol) Brushes

Cite this: Langmuir 2018, 34, 46, 13946–13955
Publication Date (Web):October 24, 2018
https://doi.org/10.1021/acs.langmuir.8b02774
Copyright © 2018 American Chemical Society

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    Abstract

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    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.

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    Cited By

    This article is cited by 2 publications.

    1. Lukas Bange, Tetiana Mukhina, Giovanna Fragneto, Valeria Rondelli, Emanuel Schneck. Influence of adhesion-promoting glycolipids on the structure and stability of solid-supported lipid double-bilayers. Soft Matter 2024, 20 (9) , 2113-2125. https://doi.org/10.1039/D3SM01615C
    2. Weiwei Tang, Zhe Zhang, Yufeng Li. Applications of carbon quantum dots in lubricant additives: a review. Journal of Materials Science 2021, 56 (21) , 12061-12092. https://doi.org/10.1007/s10853-021-06032-8

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