Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/4886
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dc.contributor.authorWiogo, Hilda T. R.-
dc.contributor.authorLim, May-
dc.contributor.authorBulmuş, Volga-
dc.contributor.authorGutie´rrez, Lucía-
dc.contributor.authorWoodward, Robert C.-
dc.contributor.authorAmal, Rose-
dc.date.accessioned2017-02-23T07:38:55Z-
dc.date.available2017-02-23T07:38:55Z-
dc.date.issued2012-03-
dc.identifier.citationWiogo, H. T. R., Lim, M., Bulmuş, V., Gutiérrez, L., Woodward, R. C., and Amal, R. (2012). Insight into serum protein interactions with functionalized magnetic nanoparticles in biological media. Langmuir, 28(9), 4346-4356. doi:10.1021/la204740ten_US
dc.identifier.issn0743-7463-
dc.identifier.issn1520-5827-
dc.identifier.urihttp://doi.org/10.1021/la204740t-
dc.identifier.urihttp://hdl.handle.net/11147/4886-
dc.description.abstractSurface modification with linear polymethacrylic acid (20 kDa), linear and branched polyethylenimine (25 kDa), and branched oligoethylenimine (800 Da) is commonly used to improve the function of magnetite nanoparticles (MNPs) in many biomedical applications. These polymers were shown herein to have different adsorption capacity and anticipated conformations on the surface of MNPs due to differences in their functional groups, architectures, and molecular weight. This in turn affects the interaction of MNPs surfaces with biological serum proteins (fetal bovine serum). MNPs coated with 25 kDa branched polyethylenimine were found to attract the highest amount of serum protein while MNPs coated with 20 kDa linear polymethacrylic acid adsorbed the least. The type and amount of protein adsorbed, and the surface conformation of the polymer was shown to affect the size stability of the MNPs in a model biological media (RPMI-1640). A moderate reduction in r 2 relaxivity was also observed for MNPs suspended in RPMI-1640 containing serum protein compared to the same particles suspended in water. However, the relaxivities following protein adsorption are still relatively high making the use of these polymer-coated MNPs as Magnetic Resonance Imaging (MRI) contrast agents feasible. This work shows that through judicious selection of functionalization polymers and elucidation of the factors governing the stabilization mechanism, the design of nanoparticles for applications in biologically relevant conditions can be improved. © 2012 American Chemical Society.en_US
dc.description.sponsorshipARC (DP0985848); Spanish ISCIII-MSPS (CD09/00030)en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofLangmuiren_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectProteinsen_US
dc.subjectBiological mediaen_US
dc.subjectStabilization mechanismsen_US
dc.subjectMagnetic nanoparticlesen_US
dc.subjectProtein adsorptionen_US
dc.titleInsight into serum protein interactions with functionalized magnetic nanoparticles in biological mediaen_US
dc.typeArticleen_US
dc.authoridTR181383en_US
dc.institutionauthorBulmuş, Volga-
dc.departmentIzmir Institute of Technology. Bioengineeringen_US
dc.identifier.volume28en_US
dc.identifier.issue9en_US
dc.identifier.startpage4346en_US
dc.identifier.endpage4356en_US
dc.identifier.wosWOS:000301038000038en_US
dc.identifier.scopus2-s2.0-84857879296en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1021/la204740t-
dc.identifier.pmid22313424en_US
dc.relation.doi10.1021/la204740ten_US
dc.coverage.doi10.1021/la204740ten_US
dc.identifier.scopusqualityQ1-
item.openairetypeArticle-
item.languageiso639-1en-
item.fulltextWith Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextopen-
crisitem.author.dept03.01. Department of Bioengineering-
Appears in Collections:Chemical Engineering / Kimya Mühendisliği
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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