Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/10749
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dc.contributor.authorWiogo, Hilda T. R.-
dc.contributor.authorLim, May-
dc.contributor.authorBulmuş, Volga-
dc.contributor.authorYun, Jimmy-
dc.contributor.authorAmal, Rose-
dc.date.accessioned2021-01-24T18:47:46Z-
dc.date.available2021-01-24T18:47:46Z-
dc.date.issued2011-
dc.identifier.issn0743-7463-
dc.identifier.issn1520-5827-
dc.identifier.urihttps://doi.org/10.1021/la104278m-
dc.identifier.urihttps://hdl.handle.net/11147/10749-
dc.descriptionPubMed: 21171579en_US
dc.description.abstractA 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.sponsorshipAustralian Research CouncilAustralian Research Councilen_US
dc.description.sponsorshipThis 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.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofLangmuiren_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.titleStabilization of magnetic iron oxide nanoparticles in biological media by fetal bovine serum (FBS)en_US
dc.typeArticleen_US
dc.institutionauthorBulmuş, Volga-
dc.departmentİzmir Institute of Technology. Bioengineeringen_US
dc.identifier.volume27en_US
dc.identifier.issue2en_US
dc.identifier.startpage843en_US
dc.identifier.endpage850en_US
dc.identifier.wosWOS:000285990500049en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1021/la104278m-
dc.identifier.pmid21171579en_US
dc.relation.doi10.1021/la104278men_US
dc.coverage.doi10.1021/la104278men_US
dc.identifier.wosqualityQ2-
dc.identifier.scopusqualityQ2-
dc.identifier.wosqualityttpTop10%en_US
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.openairetypeArticle-
crisitem.author.dept03.01. 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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