Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle Series

Polymer nanoparticles continue to be of high interest in life science applications. Still, adsorption processes occurring in protein-containing media and their implications for biological responses are not generally predictable. Here, the effect of nanoparticle composition on the adsorption of bovin...

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Main Authors: Barbara Seifert, Stefan Baudis, Christian Wischke
Format: Article
Language:English
Published: MDPI AG 2023-11-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/24/22/16390
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author Barbara Seifert
Stefan Baudis
Christian Wischke
author_facet Barbara Seifert
Stefan Baudis
Christian Wischke
author_sort Barbara Seifert
collection DOAJ
description Polymer nanoparticles continue to be of high interest in life science applications. Still, adsorption processes occurring in protein-containing media and their implications for biological responses are not generally predictable. Here, the effect of nanoparticle composition on the adsorption of bovine serum albumin (BSA), fibronectin (FN) and immunoglobulin G (IgG) as structurally and functionally different model proteins was explored by systematically altering the composition of poly(methyl methacrylate-<i>co</i>-styrene) nanoparticles with sizes in a range of about 550 nm. As determined by protein depletion from the suspension medium via a colorimetric assay, BSA and IgG adsorbed at similar quantities, while FN reached larger masses of adsorbed protein (up to 0.4 ± 0.06 µg·cm<sup>−2</sup> BSA, 0.42 ± 0.09 µg·cm<sup>−2</sup> IgG, 0.72 ± 0.04 µg·cm<sup>−2</sup> FN). A higher content of styrene as the more hydrophobic polymer component enhanced protein binding, which suggests a contribution of hydrophobic interactions despite the particles exhibiting strongly negatively charged surfaces with zeta potentials of −44 to −52 mV. The quantities of adsorbed proteins were estimated to correspond to a confluent surface coverage. Overall, this study illustrated how protein binding can be controlled by systematically varying the nanoparticle bulk composition and may serve as a basis for establishing interfaces with a targeted level of protein retention and/or presentation.
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spelling doaj.art-6db09f1bd327476ab364a21fae0cc10e2023-11-24T14:47:24ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-11-0124221639010.3390/ijms242216390Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle SeriesBarbara Seifert0Stefan Baudis1Christian Wischke2Institute of Active Polymers, Helmholtz-Zentrum Hereon, 14513 Teltow, GermanyInstitute of Active Polymers, Helmholtz-Zentrum Hereon, 14513 Teltow, GermanyInstitute of Active Polymers, Helmholtz-Zentrum Hereon, 14513 Teltow, GermanyPolymer nanoparticles continue to be of high interest in life science applications. Still, adsorption processes occurring in protein-containing media and their implications for biological responses are not generally predictable. Here, the effect of nanoparticle composition on the adsorption of bovine serum albumin (BSA), fibronectin (FN) and immunoglobulin G (IgG) as structurally and functionally different model proteins was explored by systematically altering the composition of poly(methyl methacrylate-<i>co</i>-styrene) nanoparticles with sizes in a range of about 550 nm. As determined by protein depletion from the suspension medium via a colorimetric assay, BSA and IgG adsorbed at similar quantities, while FN reached larger masses of adsorbed protein (up to 0.4 ± 0.06 µg·cm<sup>−2</sup> BSA, 0.42 ± 0.09 µg·cm<sup>−2</sup> IgG, 0.72 ± 0.04 µg·cm<sup>−2</sup> FN). A higher content of styrene as the more hydrophobic polymer component enhanced protein binding, which suggests a contribution of hydrophobic interactions despite the particles exhibiting strongly negatively charged surfaces with zeta potentials of −44 to −52 mV. The quantities of adsorbed proteins were estimated to correspond to a confluent surface coverage. Overall, this study illustrated how protein binding can be controlled by systematically varying the nanoparticle bulk composition and may serve as a basis for establishing interfaces with a targeted level of protein retention and/or presentation.https://www.mdpi.com/1422-0067/24/22/16390nanoparticlesprotein interactionpoly(methyl methacrylate-<i>co</i>-styrene)carrier systems
spellingShingle Barbara Seifert
Stefan Baudis
Christian Wischke
Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle Series
International Journal of Molecular Sciences
nanoparticles
protein interaction
poly(methyl methacrylate-<i>co</i>-styrene)
carrier systems
title Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle Series
title_full Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle Series
title_fullStr Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle Series
title_full_unstemmed Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle Series
title_short Composition-Dependent Protein–Material Interaction of Poly(Methyl Methacrylate-<i>co</i>-styrene) Nanoparticle Series
title_sort composition dependent protein material interaction of poly methyl methacrylate i co i styrene nanoparticle series
topic nanoparticles
protein interaction
poly(methyl methacrylate-<i>co</i>-styrene)
carrier systems
url https://www.mdpi.com/1422-0067/24/22/16390
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AT stefanbaudis compositiondependentproteinmaterialinteractionofpolymethylmethacrylateicoistyrenenanoparticleseries
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