PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7645
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Article Citation - WoS: 1Citation - Scopus: 1Ferromagnetism Above 200 K in Organic-Ion Intercalated CrSBr(American Chemical Society, 2025) Ferreira-Teixeira, S.; Tezze, D.; Ramos, M.; Álvarez-García, C.; Bayındır, B.; Jo, J.; Gobbi, M.CrSBr is a van der Waals magnetic semiconductor exhibiting antiferromagnetic order below 140 K. It has emerged as a promising platform for engineering 2D magnetism because its intertwined electronic, optical, and magnetic properties can be profoundly modified via external stimuli such as electrical gating or magnetic fields. However, other strategies for tuning magnetism in layered materials, such as molecular intercalation, remain largely unexplored for CrSBr. Here, we demonstrate that the intercalation of tetramethylammonium (TMA) and tetrapropylammonium (TPA) ions into CrSBr induces a transition from antiferromagnetic to ferromagnetic order, while significantly enhancing the magnetic transition temperature to 190 K (TMA) and 230 K (TPA). The resulting intercalates are air-stable and exhibit large, hysteretic magnetoresistance exceeding 60% at 50 K in the TPA case. Besides, intercalation introduces symmetry-breaking structural changes in each CrSBr plane, revealed by Raman microscopy and corroborated by density functional theory (DFT) calculations. These findings highlight molecular intercalation as a powerful and versatile route to tailor the magnetic properties of CrSBr and unlock its potential to fabricate robust, high-temperature 2D magnetic devices. © 2025 Elsevier B.V., All rights reserved.Article Silver-Loaded Titania-Based Metal-Organic Frameworks as a Platform for Silver Ion Release for Antibacterial Applications(American Chemical Society, 2025) Mazare, Anca; Goldmann, Wolfgang Heinrich; Kocak, Esra; Osuagwu, Benedict; Qin, Shanshan; Cao, Ran; Schmuki, PatrikConventional Ag-decorated TiO<inf>2</inf>coatings suffer from low adsorption capacity and burst release kinetics, limiting long-term antibacterial efficacy and risking cytotoxicity. An entirely different payload release approach can be based on metal–organic frameworks (MOFs), which offer tunable porosity, high surface area, and internal diffusion channels. Here, we report a thermally stabilized Ti-based MOF [NH<inf>2</inf>-MIL-125(Ti)] functionalized with Ag+via reactive deposition, enabling high Ag loading (∼14.7 wt %) and sustained release. Annealing at 250 °C enhances aqueous stability, allowing diffusion-governed Ag+delivery over >48 h, with 77% of the Ag still present in the MOF after a 24 h release. The system exhibits dose-dependent antibacterial activity in powders and comparable efficacy in coatings, with a more gradual release profile. This scalable platform is promising for long-acting coatings, wound interfaces, and implantable materials. © 2025 Elsevier B.V., All rights reserved.Article Citation - WoS: 111Stabilization of Magnetic Iron Oxide Nanoparticles in Biological Media by Fetal Bovine Serum (fbs)(American Chemical Society, 2011) Wiogo, Hilda T. R.; Lim, May; Bulmuş, Volga; Yun, Jimmy; Amal, RoseA 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.