Interaction between Proteins and Ir Based CO Releasing Molecules: Mechanism of Adduct Formation and CO Release(399 views) Petruk AA, Vergara A, Marasco D, Bikiel D, Doctorovich F, Estrin DA, Merlino A
Departamento de Química Inorgánica, Analítica y Química Física, University of Buenos Aires, Ciudad Universitaria, Pab. 2Buenos Aires, Argentina
Department of Chemical Sciences, University of Naples Federico II, via CintiaNapoli, Italy
CNR Institute of Biostructures and Bioimages, Via Mezzocannone 16Napoli, Italy
Department of Pharmacy, CIRPEB: Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Via Mezzocannone, 16Napoli, Italy
Departamento de Quimica Inorganica, Analitica y Quimica Fisica/INQUIMAE-CONICET, University of Buenos Aires , Ciudad Universitaria, Pab. 2, C1428EHA Buenos Aires, Argentina.
Departamento de Qu mica Inorg nica, Anal tica y Qu mica F sica, University of Buenos Aires, Ciudad Universitaria, Pab. 2Buenos Aires, Argentina
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Interaction between Proteins and Ir Based CO Releasing Molecules: Mechanism of Adduct Formation and CO Release
Carbon monoxide releasing molecules (CORMs) have important bactericidal, anti-inflammatory, neuroprotective, and antiapoptotic effects and can be used as tools for CO physiology experiments, including studies on vasodilation. In this context, a new class of CO releasing molecules, based on pentachlorocarbonyliridate(III) derivative have been recently reported. Although there is a growing interest in the characterization of protein-CORMs interactions, only limited structural information on CORM binding to protein and CO release has been available to date. Here, we report six different crystal structures describing events ranging from CORM entrance into the protein crystal up to the CO release and a biophysical characterization by isothermal titration calorimetry, Raman microspectroscopy, and molecular dynamics simulations of the complex between a pentachlorocarbonyliridate(III) derivative and hen egg white lysozyme, a model protein. Altogether, the data indicate the formation of a complex in which the ligand can bind to different sites of the protein surface and provide clues on the mechanism of adduct formation and CO release.
Interaction between Proteins and Ir Based CO Releasing Molecules: Mechanism of Adduct Formation and CO Release
Petraglia F, Singh AA, Carafa V, Nebbioso A, Conte M, Scisciola L, Valente S, Baldi A, Mandoli A, Petrizzi VB, Ingenito C, De Falco S, Cicatiello V, Apicella I, Janssen-megens EM, Kim B, Yi G, Logie C, Heath S, Ruvo M, Wierenga ATJ, Flicek P, Yaspo ML, Della Valle V, Bernard O, Tomassi S, Novellino E, Feoli A, Sbardella G, Gut I, Vellenga E, Stunnenberg HG, Mai A, Martens JHA, Altucci L * Combined HAT/EZH2 modulation leads to cancer-selective cell death(284 views) Oncotarget (ISSN: 1949-2553electronic, 1949-2553linking), 2018 May 22; 9(39): 25630-25646. Impact Factor:5.008 ViewExport to BibTeXExport to EndNote
Hesse B, Tagil K, Cuocolo A, Anagnostopoulos C, Bardies M, Bax J, Bengel F, Busemann Sokole E, Davies G, Dondi M, Edenbrandt L, Franken P, Kjaer A, Knuuti J, Lassmann M, Ljungberg M, Marcassa C, Marie PY, Mckiddie F, O'connor M, Prvuolovich E, Underwood R * 3. 0 T perfusion MR imaging(694 views) Rivista Di Neuroradiologia (ISSN: 1120-9976), 2004; 17(6): 807-812. Impact Factor:0.023 ViewExport to BibTeXExport to EndNote