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https://hdl.handle.net/11147/10749
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Wiogo, Hilda T. R. | - |
dc.contributor.author | Lim, May | - |
dc.contributor.author | Bulmuş, Volga | - |
dc.contributor.author | Yun, Jimmy | - |
dc.contributor.author | Amal, Rose | - |
dc.date.accessioned | 2021-01-24T18:47:46Z | - |
dc.date.available | 2021-01-24T18:47:46Z | - |
dc.date.issued | 2011 | - |
dc.identifier.issn | 0743-7463 | - |
dc.identifier.issn | 1520-5827 | - |
dc.identifier.uri | https://doi.org/10.1021/la104278m | - |
dc.identifier.uri | https://hdl.handle.net/11147/10749 | - |
dc.description | PubMed: 21171579 | en_US |
dc.description.abstract | A facile method of stabilizing magnetic iron oxide nanoparticles (MNPs) in biological media (RPMI-1640) via surface modification with fetal bovine scrum (FBS) is presented herein. Dynamic light scattering (DLS) shows that the size of the MNP aggregates can be maintained at 190 +/- 2 nm for up to 16 h in an RPMI 1640 culture medium containing >= 4 vol % FBS. Under transmission electron microscopy (TEM), a layer of protein coating is observed to cover the MNP surface following treatment with FBS. The adsorption of proteins is further confirmed by X-ray photoelectron spectroscopy (XPS). Gel electrophoresis and LC-MS/MS studies reveal that complement factor I-I, antithrombin, complement factor I, alpha-1-antiproteinase, and apolipoprotein E are the proteins most strongly attached to the surface of all MNP. These surface-adsorbed proteins serve as a linker that aids the adsorption of other serum proteins, such as albumin, which otherwise adsorb poorly onto MNPs. The size stability of FBS-treated MNPs in biological media is attributed to the secondary adsorbed proteins, and the size stability in biological media can be maintained only when both the surface-adsorbed proteins and the secondary adsorbed proteins are present on the particle's surface. | en_US |
dc.description.sponsorship | Australian Research CouncilAustralian Research Council | en_US |
dc.description.sponsorship | This work was financially supported by the Australian Research Council through the ARC Centre of Excellence program. We thank Dr. Ling Zhong from the Bioanalytical Mass Spectrometry Facility (BMSF, UNSW) for her assistance with LC-MS/MS analysis and Dr. Christopher Marquis and Miss Roslyn Tedja from the School of Biotechnology and Biomolecular Sciences (BABS, UNSW) for their instruction in protein gel electrophoresis. | en_US |
dc.language.iso | en | en_US |
dc.publisher | American Chemical Society | en_US |
dc.relation.ispartof | Langmuir | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.title | Stabilization of magnetic iron oxide nanoparticles in biological media by fetal bovine serum (FBS) | en_US |
dc.type | Article | en_US |
dc.institutionauthor | Bulmuş, Volga | - |
dc.department | İzmir Institute of Technology. Bioengineering | en_US |
dc.identifier.volume | 27 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.startpage | 843 | en_US |
dc.identifier.endpage | 850 | en_US |
dc.identifier.wos | WOS:000285990500049 | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.identifier.doi | 10.1021/la104278m | - |
dc.identifier.pmid | 21171579 | en_US |
dc.relation.doi | 10.1021/la104278m | en_US |
dc.coverage.doi | 10.1021/la104278m | en_US |
dc.identifier.wosquality | Q2 | - |
dc.identifier.scopusquality | Q2 | - |
dc.identifier.wosqualityttp | Top10% | en_US |
item.fulltext | No Fulltext | - |
item.grantfulltext | none | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.openairetype | Article | - |
crisitem.author.dept | 03.01. Department of Bioengineering | - |
Appears in Collections: | PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection |
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