986 resultados para 6-coordinate Copper(ii)


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The isostructural title compounds, {(C7H7N2)2[SnI4]}n, (1), and {(C7H5F2N2)2[SnI4]}n, (2), show a layered perovskite-type structure composed of anionic {[SnI4]2-}n sheets parallel to (100), which are decorated on both sides with templating benzimidazolium or 5,6-di­fluoro­benzimidazolium cations, respectively. These planar organic heterocycles mainly form N-H...I hydrogen bonds to the terminal I atoms of the corner-sharing [SnI6] octa­hedra (point group symmetry 2) from the inorganic layer, but not to the bridging ones. This is in contrast to most of the reported structures of related compounds where ammonium cations are involved. Here hydrogen bonding to both types of iodine atoms and thereby a distortion of the inorganic layers to various extents is observed. For (1) and (2), all Sn-I-Sn angles are linear and no out-of-plane distortions of the inorganic layers occur, a fact of relevance in view of the material properties. The arrangement of the aromatic cations is mainly determined through the direction of the N-H...I hydrogen bonds. The coherence between organic bilayers along [100] is mainly achieved through van der Waals inter­actions.

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The gastrin-releasing peptide receptor (GRPr) is an important molecular target for the visualization and therapy of tumors and can be targeted with radiolabeled bombesin derivatives. The present study aims to develop statine-based bombesin receptor antagonists suitable for labeling with 64Cu for imaging by positron emission tomography (PET). The potent GRPr antagonist D-Phe-Gln-Trp-Ala-Val-Gly-His-Sta-Leu-NH2 was conjugated to the sarcophagine (3,6,10,13,16,19-hexaazabicyclo[6.6.6] icosane=Sar) derivative 5-(8-methyl-3,6,10,13,16,19-hexaaza-bicyclo[6.6.6]icosan-1-ylamino)-5-oxopentanoic acid (MeCOSar) via PEG4 (LE1) and PEG2 (LE2) spacers and radiolabeled with 64Cu2+ with >95% yield and specific activities of about 100 MBq/nmol. Both Cu(II) conjugates have high affinity for GRPr (IC50: natCu-LE1, 1.4±0.1 nM; natCu-LE2, 3.8±0.6 nM). The antagonistic properties of both conjugates were confirmed by Ca2+-flux measurements. Biodistribution studies of Cu-64-LE1 exhibited specific targeting of the tumor (19.6±4.7% IA/g at 1 h p.i.) and GRPr-positive organs. Biodistribution and PET images at 4 and 24 h postinjection showed increasing tumor-to-background ratios with time. This was illustrated by the acquisition of PET images showing high tumor-to-normal tissue contrast. This study demonstrates the high affinity of the MeCOSar-PEGx-bombesin conjugates to GRPr. The stability of 64Cu complexes of MeCOSar, the long half-life of 64Cu, and the suitable biodistribution profile of the 64Cu-labeled peptides lead to PET images of high contrast suitable for potential translation into the clinic.

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5 Briefe zwischen C. C. Eckhardt und Max Horkheimer, 1942; 41 Briefe und Beilage zwischen Lilly Eckmeyer und Max Horkheimer, 1947-1950; 1 Brief und Beilage von Max Horkheimer an das Colegio de Mexico, 1943; 15 Briefe zwischen K. Heiner Emhardt und Max Horkheimer, 1945-1948; 8 Briefe und Beilage zwischen Ernst Engelberg und Max Horkheimer, 1946-1947; 5 Briefe zwischen Gertrude Speer und Max Horkheimer, 1946 siehe auch Ernst Engelberg; 1 Brief von Max Horkheimer an Erik H. Erikson, 1946; 2 Briefe und Beilage zwischen Esprit [Zeitschrift] und Max Horkheimer, 1947, 1948;

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Signatur des Originals: S 36/F07552

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Trägerband: Ms. Praed. 109; Vorbesitzer: Dominikanerkloster Frankfurt am Main

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Trägerbände: Ms. Barth. 26; Ms. Barth. 29; Vorbesitzer: Bartholomaeusstift Frankfurt am Main

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Fil: Pedernera, Soledad. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.

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Fil: Pedernera, Soledad. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.