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Title: Insight into serum protein interactions with functionalized magnetic nanoparticles in biological media
Authors: Wiogo, Hilda T. R.
Lim, May
Bulmuş, Volga
Gutie´rrez, Lucía
Woodward, Robert C.
Amal, Rose
Keywords: Proteins
Biological media
Stabilization mechanisms
Magnetic nanoparticles
Protein adsorption
Issue Date: Mar-2012
Publisher: American Chemical Society
Source: Wiogo, 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/la204740t
Abstract: Surface 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.
ISSN: 0743-7463
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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