Rhenium(V) oxo complexes with acetylacetone derived schiff bases: Structure and catalytic epoxidation
INORGANIC CHEMISTRY
Authors: Sachse, Anna; Mosch-Zanetti, Nadia C.; Lyashenko, Ganna; Wielandt, J. Wolfram; Most, Kerstin; Magull, Jorg; Dall'Antonia, Fabio; Pal, Aritra; Herbst-Irmer, Regine
Abstract
Substitution reactions of rhenium(V) oxo precursors [ReOC13(PPh3)21 or [NBU4][ReOC141 with the bidentate acetylacetone-d e rived ketoamine ligands APOH = 4-anilino-3-penten-2-one, DPOH = 4-[2,6-dimethylanilino]-3penten-2-one, and MTPOH = 4-[2-(methylthio)anilinol-3-penten-2-one gave the complexes [ReO(APO)CI2(PPh3)] (1), [ReO(DPO)C]2(PPh3)] (2), and [NBU4][ReOLCI31 (3, L = APO; 4, L = DPO; 5, L = MTPO), respectively. All complexes exhibit only one ketoamino chelate, independent of the amount of ligand added to the rhenium precursors. The complexes were characterized by 1H and 13C NMR spectroscopy. X-ray crystal structures of the complexes 1, 2, 4, and 5, including that of MTPOH, were determined, revealing the trans position of the two oxygen atoms and the trans-CI,Cl conformation in 1 and 2, in contrast to most other rhenium complexes of this type where the cis-CI,Cl conformation is observed. Coordination of the potentially tridentate ligand MTPOH in 5 is bidentate with a dangling thioether substituent. Compound 2 shows catalytic activity in the oxidation of cis-cyclooctene with tertbuty1hydroperoxide.
Interactions between Hepatitis C Virus and the Human Apolipoprotein H Acute Phase Protein: A Tool for a Sensitive Detection of the Virus
PLOS ONE
Authors: Stefas, Ilias; Tigrett, Sylvia; Dubois, Gregor; Kaiser, Marco; Lucarz, Estelle; Gobby, Delphine; Bray, Dorothy; Ellerbrok, Heinz; Zarski, Jean Pierre; Veas, Francisco
Abstract
The Hepatitis C virus (HCV) infection exhibits a high global prevalence frequently associated with hepatocellular carcinoma, taking years to develop. Despite the standardization of highly sensitive HCV quantitative RT-PCR (qRT-PCR) detection methods, false-negative diagnoses may be generated with current methods, mainly due to the presence of PCR inhibitors and/or low viral loads in the patient's sample. These false-negative diagnoses impact both public health systems, in developing countries, and an in lesser extent, in developed countries, including both the risk of virus transmission during organ transplantation and/or blood transfusion and the quality of the antiviral treatment monitoring. To adopt an appropriate therapeutic strategy to improve the patient's prognosis, it is urgent to increase the HCV detection sensitivity. Based upon previous studies on HBV, we worked on the capacity of the scavenger acute phase protein, Apolipoprotein H (ApoH) to interact with HCV. Using different approaches, including immunoassays, antibody-inhibition, oxidation, ultracentrifugation, electron microscopy and RT-PCR analyses, we demonstrated specific interactions between HCV particles and ApoH. Moreover, when using a two-step HCV detection process, including capture of HCV by ApoH-coated nanomagnetic beads and a home-made real-time HCV-RT-PCR, we confirmed the presence of HCV for all samples from a clinical collection of HCV-seropositive patients exhibiting an RT-PCR COBAS (R) Taq-Man (R) HCV Test, v2.0 (COBAS)-positive result. In contrast, for HCV-seropositive patients with either low HCV-load as determined with COBAS or exhibiting HCV-negative COBAS results, the addition of the two-step ApoH-HCV-capture and HCV-detection process was able to increase the sensitivity of HCV detection or more interestingly, detect in a genotype sequence-independent manner, a high-proportion (44%) of HCV/RNA-positive among the COBAS HCV-negative patients. Thus, the immune interaction between ApoH and HCV could be used as a sample preparation tool to enrich and/or cleanse HCV patient's samples to enhance the detection sensitivity of HCV and therefore significantly reduce the numbers of false-negative HCV diagnosis results.