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http://dx.doi.org/10.25673/113040
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DC Element | Wert | Sprache |
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dc.contributor.author | Seifert, Barbara | - |
dc.contributor.author | Baudis, Stefan | - |
dc.contributor.author | Wischke, Christian | - |
dc.date.accessioned | 2024-01-15T09:44:20Z | - |
dc.date.available | 2024-01-15T09:44:20Z | - |
dc.date.issued | 2023 | - |
dc.identifier.uri | https://opendata.uni-halle.de//handle/1981185920/114996 | - |
dc.identifier.uri | http://dx.doi.org/10.25673/113040 | - |
dc.description.abstract | 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-co-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−2 BSA, 0.42 ± 0.09 µg·cm−2 IgG, 0.72 ± 0.04 µg·cm−2 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. | eng |
dc.language.iso | eng | - |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | - |
dc.subject.ddc | 615 | - |
dc.title | Composition-dependent protein-material interaction of Poly(Methyl Methacrylate-co-styrene) nanoparticle series | eng |
dc.type | Article | - |
local.versionType | publishedVersion | - |
local.bibliographicCitation.journaltitle | International journal of molecular sciences | - |
local.bibliographicCitation.volume | 24 | - |
local.bibliographicCitation.pagestart | 1 | - |
local.bibliographicCitation.pageend | 11 | - |
local.bibliographicCitation.publishername | Molecular Diversity Preservation International | - |
local.bibliographicCitation.publisherplace | Basel | - |
local.bibliographicCitation.doi | 10.3390/ijms242216390 | - |
local.subject.keywords | nanoparticles; protein interaction; poly(methyl methacrylate-co-styrene); carrier systems | - |
local.openaccess | true | - |
dc.identifier.ppn | 1878064347 | - |
cbs.publication.displayform | 2023 | - |
local.bibliographicCitation.year | 2023 | - |
cbs.sru.importDate | 2024-01-15T09:43:55Z | - |
local.bibliographicCitation | Enthalten in International journal of molecular sciences - Basel : Molecular Diversity Preservation International, 2000 | - |
local.accessrights.dnb | free | - |
Enthalten in den Sammlungen: | Open Access Publikationen der MLU |
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Datei | Beschreibung | Größe | Format | |
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ijms-24-16390.pdf | 5.56 MB | Adobe PDF | ![]() Öffnen/Anzeigen |