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Sökning: WFRF:(Neels Antonia)

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1.
  • Heckenroth, Marion, et al. (författare)
  • Catalytic Hydrogenation Using Abnormal N-Heterocyclic Carbene Palladium Complexes: Catalytic Scope and Mechanistic Insights
  • 2011
  • Ingår i: ChemCatChem. - : Wiley. - 1867-3880. ; 3:1, s. 167-173
  • Tidskriftsartikel (refereegranskat)abstract
    • Palladium complexes containing abnormally bound C4-bound dicarbene ligands have been exploited for catalytic alkene hydrogenation. Comparison to normally C2-bound homologues indicates that the carbene bonding mode critically influences the catalytic activity. Good catalytic performance in the hydrogenation of cis-disubstituted olefins and non-isomerizable terminal olefins under mild conditions (RT, 0.1 MPa H-2) only occurs when the carbene is abnormally bound to the palladium center. Detailed mechanistic investigations using dynamic light scattering in connection with time-dependent analysis of conversions, and also performance of substoichiometric catalytic experiments provide evidence that the catalysis is heterogeneous and that the abnormally bound carbene ligand has the role of an activator.
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2.
  • Iranpour Anaraki, Neda, et al. (författare)
  • In-situ Investigations on Gold Nanoparticles Stabilization Mechanisms in Biological Environments Containing HSA
  • 2022
  • Ingår i: Advanced Functional Materials. - : Wiley. - 1616-3028 .- 1616-301X. ; 32:9
  • Tidskriftsartikel (refereegranskat)abstract
    • Nanoparticles (NPs) developments advance innovative biomedical applications. However, complex interactions and the low colloidal stability of NPs in biological media restrict their widespread utilization. The influence of NPs properties on the colloidal stability for gold NPs with 5 and 40 nm in diameter with two surface modifications, methoxy-polyethylene glycol-sulfhydryl (PEG) and citrate, in NaCl and human serum albumin (HSA) protein solution, is investigated. This study is based on small-angle X-ray scattering (SAXS) methods allowing the in-situ monitoring of interactions in physiological conditions. The PEG coating provides high colloidal stability for NPs of both sizes. For 5 nm NPs in NaCl solution, a stable 3D self-assembled body-centered cubic (BCC) arrangement is detected with an interparticle distance of 20.7 ± 0.1 nm. In protein solution, this distance increases to 21.9 ± 0.1 nm by protein penetration inside the ordered structure. For citrate-capped NPs, a different mechanism is observed. The protein particles attach to the NPs surfaces, and an appropriate concentration of proteins results in a stable suspension. Cryogenic transmission electron microscopy (Cryo-TEM), UV–visible spectroscopy, and dynamic light scattering (DLS) support the SAXS results. The findings will pave the way to design and synthesize NPs with controlled behaviors in biomedical applications.
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