TY - JOUR AB - Fabrication of magnetic nanocomposites containing iron oxide nanoparticles formed in situ within a phosphorus-containing polymer matrix as well as its structural characterization and its thermal degradation is reported here. Comparative structural studies of the parent polymer and nanocomposites were performed using FTIR spectroscopy, x-ray diffraction, and atomic force microscopy. The results confirmed the presence of dispersed iron oxide magnetic nanoparticles in the polymer matrix. The formed composite combines the properties of porous polymer carriers and magnetic particles enabling easy separation and reapplication of such polymeric carriers used in, for example, catalysis or environmental remediation. Studies on thermal degradation of the composites revealed that the process proceeds in three stages while a significant influence of the embedded magnetic particles on that process was observed in the first two stages. Magnetic force microscopy studies revealed that nanocomposites and its calcinated form have strong magnetic properties. The obtained results provide a comprehensive characterization of magnetic nanocomposites and the products of their calcination that are important for their possible applications as sorbents (regeneration conditions, processing temperature, disposal, etc). AU - Alosmanov, R.* AU - Szuwarzyński, M.* AU - Schnelle-Kreis, J. AU - Matuschek, G. AU - Magerramov, A.M.* AU - Azizov, A.A.* AU - Zimmermann, R. AU - Zapotoczny, S.* C1 - 52832 C2 - 44495 CY - Bristol TI - Magnetic nanocomposites based on phosphorus-containing polymers -structural characterization and thermal analysis. JO - Nanotechnol. VL - 29 IS - 13 PB - Iop Publishing Ltd PY - 2018 SN - 0957-4484 ER - TY - JOUR AB - When nanoparticles (NP) enter the body they come into contact with body fluids containing proteins which can adsorb to their surface. These proteins may influence the NP interactions with the biological vicinity, eventually determining their biological fate inside the body. Adsorption of the most abundantly binding proteins was studied after an in vitro 24 hr incubation of monodisperse, negatively charged 5, 15 and 80 nm gold spheres (AuNP) in mouse serum by a two-step analysis: proteomic protein identification and quantitative protein biochemistry. The adsorbed proteins were separated from non-adsorbed proteins by centrifugation and gel electrophoresis and identified using a MALDI-TOF-MS-Proteomics-Analyzer. Quantitative analysis of proteins in gel bands by protein densitometry, required the focus on predominantly binding serum proteins. Numerous proteins adsorbed to the AuNP depending on their size, e.g. apolipoproteins or complement C3. The qualitative and quantitative amount of adsorbed proteins differed between 5, 15 and 80 nm AuNP. Band intensities of adsorbed proteins decreased with increasing AuNP sizes based not only on their mass but also on their surface area. Summarizing, the AuNP surface is covered with serum proteins containing transport and immune related proteins among others. Hence, protein binding depends on the size, surface area and curvature of the AuNP. AU - Schäffler, M. AU - Semmler-Behnke, M. AU - Sarioglu, H. AU - Takenaka, S. AU - Wenk, A. AU - Schleh, C. AU - Hauck, S.M. AU - Johnston, B.D. AU - Kreyling, W.G. C1 - 25908 C2 - 31990 TI - Serum protein identification and quantification of the corona of 5, 15 and 80 nm gold nanoparticles. JO - Nanotechnol. VL - 24 IS - 26 PB - Iop Publishing PY - 2013 SN - 0957-4484 ER -