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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MDPI AG
2023-11-01
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Series: | International Journal of Molecular Sciences |
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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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issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-09T16:45:01Z |
publishDate | 2023-11-01 |
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series | International Journal of Molecular Sciences |
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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