Chemical Engineering / Kimya Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/14
Browse
2 results
Search Results
Now showing 1 - 2 of 2
Article Citation - WoS: 55Citation - Scopus: 61Insight Into Serum Protein Interactions With Functionalized Magnetic Nanoparticles in Biological Media(American Chemical Society, 2012) Wiogo, Hilda T. R.; Lim, May; Bulmuş, Volga; Gutie´rrez, Lucía; Woodward, Robert C.; Amal, RoseSurface 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.Article Citation - WoS: 22Citation - Scopus: 21A Novel Silk Fibroin-Supported Iron Catalyst for Hydroxylation of Phenol(John Wiley and Sons Inc., 2006) Pekşen, Bahar Başak; Üzelakçil, Caner; Güneş, Alev; Malay, Özge; Bayraktar, OğuzThe aim of this study was to explore the potential use of silk fibroin (SF) as a catalyst support material for phenol hydroxylation reactions. Iron-substituted silk fibroin fibers were prepared using formic acid at room temperature and characterized using inductively coupled plasma atomic-emission spectrometry, scanning electron microscopy, Fourier transform infrared spectroscopy (FTIR) and optical microscopy. Measurement of an FTIR spectrum showed that the secondary structure was β-structure before and after iron substitution. To evaluate the catalytic properties of prepared catalyst, phenol hydroxylation reaction was carried out using aqueous hydrogen peroxide as an oxidant. An excellent transformation of phenol into dihydroxybenzenes (catechol and hydroquinone) was achieved. Phenol conversions of 3.3%, 61.2%, and 80.3% were obtained at room temperature, 40°C and 60°C respectively. It was found that no further phenol conversion proceeded because catalysts became separated from the reaction system during the reaction. No significant leaching of the iron was detected. Catalyst could be reused several times without a significant change in activity. Parent silk fibroin fibers without iron were inactive.