Nitrogen oxide interaction with copper complexes formed by small peptides belonging to the prion protein octa-repeat region (1115 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2007 Apr 14; (14): 1400-1408.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.212, 5-year impact factor: 3.138
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33947641676&partnerID=40&md5=9fff9885645c31d380b04db0938c233a
Keywords: Electron Transfer Mechanism, Pyramidal Structure, Zinc Powder Addition, Addition Reactions, Copper Compounds, Electron Spin Resonance Spectroscopy, Electron Transitions, Intercalation, Proteins, Nitrogen Oxides, Copper Acetyl Histidyl Glycyl Glycyl Glycinamide, Copper Acetyl Phenylalanyl Histidyl Glycyl Glycyl Glycyl Tryptophyl Glycyl Glutaminamide, Copper Acetyl-Histidyl-Glycyl-Glycyl-Glycinamide, Copper Acetyl-Phenylalanyl-Histidyl-Glycyl-Glycyl-Glycyl-Tryptophyl-Glycyl-Glutaminamide, Nitrite, Oligopeptide, Organometallic Compound, Unclassified Drug, Water, Amino Acid Sequence, Article, Chemistry, Molecular Genetics, Prion, Solution And Solubility, Molecular Sequence Data, Repetitive Sequences, Copper Chemistry, Nitrites Chemistry, Nitrogen Oxides Chemistry, Oligopeptides Chemistry, Organometallic Compounds Chemistry, Prions Chemistry, Solutions Chemistry, Water Chemistry,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita di Catania, Viale A. Doria 6, 95125, Catania, Italy. rbonomo@unict.it
Istituto di Biostrutture e Bioimmagini del CNR (Sezione di Catania), Viale A. Doria 6, 95125, Catania, Italy
References:
Not available.
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2007 Apr 14; (14): 1400-1408.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.212, 5-year impact factor: 3.138
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33947641676&partnerID=40&md5=9fff9885645c31d380b04db0938c233a
Keywords: Electron Transfer Mechanism, Pyramidal Structure, Zinc Powder Addition, Addition Reactions, Copper Compounds, Electron Spin Resonance Spectroscopy, Electron Transitions, Intercalation, Proteins, Nitrogen Oxides, Copper Acetyl Histidyl Glycyl Glycyl Glycinamide, Copper Acetyl Phenylalanyl Histidyl Glycyl Glycyl Glycyl Tryptophyl Glycyl Glutaminamide, Copper Acetyl-Histidyl-Glycyl-Glycyl-Glycinamide, Copper Acetyl-Phenylalanyl-Histidyl-Glycyl-Glycyl-Glycyl-Tryptophyl-Glycyl-Glutaminamide, Nitrite, Oligopeptide, Organometallic Compound, Unclassified Drug, Water, Amino Acid Sequence, Article, Chemistry, Molecular Genetics, Prion, Solution And Solubility, Molecular Sequence Data, Repetitive Sequences, Copper Chemistry, Nitrites Chemistry, Nitrogen Oxides Chemistry, Oligopeptides Chemistry, Organometallic Compounds Chemistry, Prions Chemistry, Solutions Chemistry, Water Chemistry,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita di Catania, Viale A. Doria 6, 95125, Catania, Italy. rbonomo@unict.it
Istituto di Biostrutture e Bioimmagini del CNR (Sezione di Catania), Viale A. Doria 6, 95125, Catania, Italy
References:
Not available.
Nitrogen oxide interaction with copper complexes formed by small peptides belonging to the prion protein octa-repeat region
The interaction between NO and copper(II) complexes formed by peptides coming from the N-terminal prion protein octa-repeat region was studied. Aqueous solutions of the Cu-Ac-HGGG-NH(2) and the Cu-Ac-PHGGGWGQ-NH(2) systems around pH 7.5 were tested after the addition of NONOates as a source of NO. UV-Vis, room temperature and frozen solution EPR spectra showed the occurrence of copper(ii) reduction in all these complexes. The reduction of these complexes is probably mediated by the formation of a labile NO adduct, which, after re-oxidation, leads to a relatively stable NO(2)(-) adduct through the apical coordination along the void site of their square pyramidal structure. In fact, the most significant shifts in EPR magnetic parameters (g(||) and A(||) or g(iso) and A(iso)) as well as in the optical parameters (lambda(max) and epsilon(max)) gave a reason for geometrical changes of the copper coordination polyhedron from a distorted square pyramid to a pseudo-octahedron. The presence of oxygen in the aqueous solution hindered the reduction ability of NO towards copper, but it made it easier to return to the original species. In order to elucidate the possible mechanism of this interaction, the reduction of copper complexed by these ligands was followed by means of zinc powder addition. The further addition of nitrite to the solution containing reduced copper led to the conclusion that nitrite could easily form an adduct, which after re-oxidation presented the same spectral features of the species obtained when the NO interaction was followed. The complexity of this interaction could involve both an inner or an outer-sphere electron transfer mechanism.
The interaction between NO and copper(II) complexes formed by peptides coming from the N-terminal prion protein octa-repeat region was studied. Aqueous solutions of the Cu-Ac-HGGG-NH(2) and the Cu-Ac-PHGGGWGQ-NH(2) systems around pH 7.5 were tested after the addition of NONOates as a source of NO. UV-Vis, room temperature and frozen solution EPR spectra showed the occurrence of copper(ii) reduction in all these complexes. The reduction of these complexes is probably mediated by the formation of a labile NO adduct, which, after re-oxidation, leads to a relatively stable NO(2)(-) adduct through the apical coordination along the void site of their square pyramidal structure. In fact, the most significant shifts in EPR magnetic parameters (g(||) and A(||) or g(iso) and A(iso)) as well as in the optical parameters (lambda(max) and epsilon(max)) gave a reason for geometrical changes of the copper coordination polyhedron from a distorted square pyramid to a pseudo-octahedron. The presence of oxygen in the aqueous solution hindered the reduction ability of NO towards copper, but it made it easier to return to the original species. In order to elucidate the possible mechanism of this interaction, the reduction of copper complexed by these ligands was followed by means of zinc powder addition. The further addition of nitrite to the solution containing reduced copper led to the conclusion that nitrite could easily form an adduct, which after re-oxidation presented the same spectral features of the species obtained when the NO interaction was followed. The complexity of this interaction could involve both an inner or an outer-sphere electron transfer mechanism.
Nitrogen oxide interaction with copper complexes formed by small peptides belonging to the prion protein octa-repeat region
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Nitrogen oxide interaction with copper complexes formed by small peptides belonging to the prion protein octa-repeat region
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* From Peptide Fragments to Whole Protein: Copper(II) Load and Coordination Features of IAPP (907 views) (PDF 164 views)
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Impact Factor: 5.16
View Export to BibTeX Export to EndNote
Magrì A, Tabbì G, Breglia R, De Gioia L, Fantucci P, Bruschi M, Bonomo RP, La Mendola D
* Copper ion interaction with the RNase catalytic site fragment of the angiogenin protein: an experimental and theoretical investigation (1435 views) (PDF 221 views)
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Impact Factor: 4.099
View Export to BibTeX Export to EndNote
Di Natale G, Osz K, Kállay C, Pappalardo G, Sanna D, Impellizzeri G, Sóvágó I, Rizzarelli E
* Affinity, speciation, and molecular features of copper(II) complexes with a prion tetraoctarepeat domain in aqueous solution: insights into old and new results (841 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2013 Mar 11; 19(11): 3751-3761.
Impact Factor: 5.696
View Export to BibTeX Export to EndNote
Travaglia A, La Mendola D, Magrì A, Nicoletti VG, Pietropaolo A, Rizzarelli E
* Copper, BDNF and Its N-terminal domain: inorganic features and biological perspectives (747 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2012 Dec 3; 18(49): 15618-15631.
Impact Factor: 5.831
View Export to BibTeX Export to EndNote
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I
* Copper(II) complexes of rat amylin fragments (730 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721.
Impact Factor: 3.838
View Export to BibTeX Export to EndNote
Grasso GI, Arena G, Bellia F, Maccarrone G, Parrinello M, Pietropaolo A, Vecchio G, Rizzarelli E
* Intramolecular weak interactions in the thermodynamic stereoselectivity of copper(II) complexes with carnosine-trehalose conjugates (826 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Sep 16; 17(34): 9448-9455.
Impact Factor: 5.925
View Export to BibTeX Export to EndNote
Vagliasindi LI, Arena G, Bonomo RP, Pappalardo G, Tabbì G
* Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein (678 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2011 Mar 21; 40(11): 2441-2450.
Impact Factor: 3.838
View Export to BibTeX Export to EndNote
La Mendola D, Magrì A, Vagliasindi LI, Hansson Ö, Bonomo RP, Rizzarelli E
* Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin (726 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2010 Nov 28; 39(44): 10678-10684.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (759 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
View Export to BibTeX Export to EndNote
Józsa E, Osz K, Kállay C, de Bona P, Damante CA, Pappalardo G, Rizzarelli E, Sóvágó I
* Nickel(ii) and mixed metal complexes of amyloid-β N-terminus (698 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010 Sep 14; 39(30): 7046-7053.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1695 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Jozsa E, Hosz K, Kallay C, De Bona P, Damante CA, Pappalardo G, Rizzarelli E, Sovago I
* Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments (833 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010; 39(30): 7046-7053.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
Bonomo RP, Di Natale G, Rizzarelli E, Tabbì G, Vagliasindi LI
* Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies (664 views)
Dalton T (ISSN: 1477-9226, 1477-7922, 1477-9234), 2009 Apr 14; (14): 2637-2646.
Impact Factor: 2.908
View Export to BibTeX Export to EndNote
Bonomo RP, Pappalardo G, Rizzarelli E, Tabbì G, Vagliasindi LI
* Studies of nitric oxide interaction with mono- and dinuclear copper(II) complexes of prion protein bis-octarepeat fragments (518 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2008 Sep 7; (29): 3805-3816.
Impact Factor: 3.58
View Export to BibTeX Export to EndNote
Osz K, Nagy Z, Pappalardo G, Di Natale G, Sanna D, Micera G, Rizzarelli E, Sóvágó I
* Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details (940 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2007; 13(25): 7129-7143.
Impact Factor: 5.33
View Export to BibTeX Export to EndNote
Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
* Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues (707 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2005 Dec 23; 12(2): 537-547.
Impact Factor: 4.907
View Export to BibTeX Export to EndNote
Arena G, Bonomo RP, Contino A, Sgarlata C, Spoto G, Tabbì G
* Influence of the coordination geometry on the physicochemical properties of a copper(II) complex with a tailor-made calixarene-based ligand bearing dipyridyl pendants. An ESR, UV-Vis and CV study (503 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2004 Oct 21; (20): 3205-3211.
Impact Factor: 2.926
View Export to BibTeX Export to EndNote
Cucinotta V, Giuffrida A, La Mendola D, Maccarrone G, Puglisi A, Rizzarelli E, Vecchio G
* 3-Amino Derivative Of Beta-Cyclodextrin: Thermodynamics Of Copper (ii) Complexes And Exploitation Of Its Enantioselectivity In The Separation Of Amino Acid Racemates By Ligand Exchange Capillary Electrophoresis (518 views)
And Life Sciencesjournal Of Chromatography B Analytical Technologies In The Biomedical, 2004 Feb 5; 800(1-2): 127-133.
Impact Factor: 1.403
View Export to BibTeX Export to EndNote
Cimino P, Improta R, Bifulco G, Riccio R, Gomez-paloma L, Barone V
* Nucleophilic Cyclopropane Ring Opening in Duocarmycin SA Derivatives by Methanol under Acid Conditions: A Quantum Mechanical Study in the Gas-Phase and in Solution (978 views)
J Org Chem (ISSN: 0022-3263, 0022-3263linking), 2004; 69(8): 2816-2824.
Impact Factor: 3.462
View Export to BibTeX Export to EndNote
Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
* Potentiometric, spectroscopic and antioxidant activity studies of SOD mimics containing carnosine (641 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
View Export to BibTeX Export to EndNote
20 Records (20 excluding Abstracts).
Total impact factor: 81.831 (81.831 excluding Abstracts).
Total 5 year impact factor: 85.267 (85.267 excluding Abstracts).
Total impact factor: 81.831 (81.831 excluding Abstracts).
Total 5 year impact factor: 85.267 (85.267 excluding Abstracts).
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