Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region
Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region(431 views visite) Brown DR, Guantieri V, Grasso G, Impellizzeri G, Pappalardo G, Rizzarelli E
Keywords Parole chiave: Copper, Peptides, Prion, Toxicity, Copper Complex, Histidine, Imidazole Derivative, Peptide Fragment, Prion Protein, Acetylation, Amidation, Amino Acid Sequence, Amino Terminal Sequence, Animal Cell, Article, Binding Site, Carboxy Terminal Sequence, Circular Dichroism, Controlled Study, Electron Spin Resonance, Electrospray Mass Spectrometry, Mouse, Nerve Cell, Nonhuman, Protein Binding, Protein Conformation, Protein Motif, Protein Structure, Stoichiometry, Ultraviolet Spectrophotometry, Amino Acid Motifs, Cultured, Electron Spin Resonance Spectroscopy, Hydrogen-Ion Concentration, Metalloproteins, Inbred Strains, Neurons, Polytetrafluoroethylene, Electrospray Ionization, Staphylococcus Phage 187,
Affiliations Affiliazioni: *** IBB - CNR ***
Dept. of Biology and Biochemistry, University of Bath, Bath BA2 7AY, United Kingdom Dipto. Chim. Inorg., M., Università di Padova, via Marzolo 1, 35131 Padova, Italy Ist. CNR Biostrutture e Bioimmagini, Sezione di Catania, V.le A. Doria 6, 95125 Catania, Italy Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 95125 Catania, Italy
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Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region
In this paper, we report the characterization of copper(II) complexes with two prion (PrP) protein peptide fragment analogues (VNITKQHTVTTTT), one with the N-terminus acetylated and the C-terminus amidated (PrP Ac180-193NH(2)) and the other with both the G and N-termini free (PrP 180-193). Such peptide sequence almost entirely encompasses the PrPC's helix 2 in the G terminal region. The stoichiometry, the binding modes and the conformational features of the copper(II) complexes with the above mentioned two peptides were investigated by electrospray ionization-mass spectrometry (ESI-MS), UV-visible (UV-Vis) spectrometry and electron paramagnetic resonance (EPR) spectrometry as well as by circular dichroism (CD) measurements. The binding site location of copper(II) in the structured region of the protein can be here suggested on the basis of our findings that show the involvement of His 187 residue. The similarity of the EPR parameters suggests that the anchoring imidazole residue drives the copper(II) coordination environment towards a common binding motif in different regions of the prion protein. (C) 2003 Elsevier Inc. All rights reserved.
Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region
Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region
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(206 visite) Oncotarget (ISSN: 1949-2553electronic, 1949-2553linking), 2018 May 22; 9(39): 25630-25646. Impact Factor:5.008 DettagliEsporta in BibTeXEsporta in EndNote
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(387 visite) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
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