Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein (500 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2011 Mar 21; 40(11): 2441-2450.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.838, 5-year impact factor: 3.887
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79952145496&partnerID=40&md5=cac70494405b7c98c2bc0ec611c99f7a
Keywords: Aqueous Solutions, Coordination Sphere, Copper Complexes, Epr Spectra, Equatorial Planes, Histidine Residues, Human Prion Protein, Hyperfine Coupling Constants, Low Temperatures, N-Terminals, Neutral Region, Nitrogen Atom, Nitrogen Donors, Oxygen Atom, Peptide Nitrogen, Ph Range, Ph Value, Pseudo-Octahedral Geometries, Redox Potentials, Spectroscopic Data, Voltammetric Studies, Water Molecule, Amino Acids, Chromophores, Coordination Reactions, Electron Spin Resonance Spectroscopy, Redox Reactions, Stereochemistry, Copper Compounds, Animal, Article, Circular Dichroism, Genetics, High Performance Liquid Chromatography, Instrumentation, Methodology, Opossum, Potentiometry, High Pressure Liquid, Spectrum Analysis, High Pressure Liquid Instrumentation Methods, Copper Chemistry, Prions Chemistry Genetics, Spectrum Analysis Methods,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125, Catania, Italy
Consorzio Interuniversitario C.I.R.C.S.M.B., Via C. Ulpiani 27, 70125, Bari, Italy
Istituto di Biostrutture e Bioimmagini, CNR, U.O.S. di Catania, Viale A. Doria 6, 95125, Catania, Italy
References:
Not available.
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2011 Mar 21; 40(11): 2441-2450.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.838, 5-year impact factor: 3.887
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79952145496&partnerID=40&md5=cac70494405b7c98c2bc0ec611c99f7a
Keywords: Aqueous Solutions, Coordination Sphere, Copper Complexes, Epr Spectra, Equatorial Planes, Histidine Residues, Human Prion Protein, Hyperfine Coupling Constants, Low Temperatures, N-Terminals, Neutral Region, Nitrogen Atom, Nitrogen Donors, Oxygen Atom, Peptide Nitrogen, Ph Range, Ph Value, Pseudo-Octahedral Geometries, Redox Potentials, Spectroscopic Data, Voltammetric Studies, Water Molecule, Amino Acids, Chromophores, Coordination Reactions, Electron Spin Resonance Spectroscopy, Redox Reactions, Stereochemistry, Copper Compounds, Animal, Article, Circular Dichroism, Genetics, High Performance Liquid Chromatography, Instrumentation, Methodology, Opossum, Potentiometry, High Pressure Liquid, Spectrum Analysis, High Pressure Liquid Instrumentation Methods, Copper Chemistry, Prions Chemistry Genetics, Spectrum Analysis Methods,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125, Catania, Italy
Consorzio Interuniversitario C.I.R.C.S.M.B., Via C. Ulpiani 27, 70125, Bari, Italy
Istituto di Biostrutture e Bioimmagini, CNR, U.O.S. di Catania, Viale A. Doria 6, 95125, Catania, Italy
References:
Not available.
Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein
A spectroscopic (UV-Vis, CD and EPR), thermodynamic and voltammetric study of the copper(II) complexes with the Ac-PHPGGSNWGQ-NH(2) polypeptide (L), a fragment of the opossum PrP protein N-terminal four-repeat region, was carried out in aqueous solution. It suggests the formation of a highly distorted [Cu(L)H(-2)] complex species in the neutral region, the stereochemistry of which is ascribable to a square base pyramid and a CuN(3)O(2) chromophore, resulting from the coordination of a histidine imidazole and two peptide nitrogen atoms and probably oxygen atoms from water molecules. At basic pH values a [Cu(L)H(-3)](-) species with a pseudo-octahedral geometry was also obtained, with four nitrogen donor atoms in its equatorial plane, coming from the histidine residue and from peptidic nitrogen atoms. Interestingly, at pH values relatively higher than the neutrality, the coordination sphere of the copper complex in the [Cu(L)H(-2)] species changes its stereochemistry towards a pseudo-octahedron, as suggested by the change in the parallel copper hyperfine coupling constant of the EPR spectra at low temperature. A slight difference in the redox potentials between this two-faced [Cu(L)H(-2)] complex species seems to confirm this behaviour. Both potentiometric and spectroscopic data were compared with the analogous species obtained with the Ac-PHGGGWGQ-NH(2) peptide, belonging to the octarepeat domain of the human prion protein (hPrP) N-terminal region. The [Cu(L)H(-2)] species formed by the Ac-PHPGGSNWGQ-NH(2) decapeptide, having a slightly lower stability, turned out to be less abundant and to exist within a narrow pH range.
A spectroscopic (UV-Vis, CD and EPR), thermodynamic and voltammetric study of the copper(II) complexes with the Ac-PHPGGSNWGQ-NH(2) polypeptide (L), a fragment of the opossum PrP protein N-terminal four-repeat region, was carried out in aqueous solution. It suggests the formation of a highly distorted [Cu(L)H(-2)] complex species in the neutral region, the stereochemistry of which is ascribable to a square base pyramid and a CuN(3)O(2) chromophore, resulting from the coordination of a histidine imidazole and two peptide nitrogen atoms and probably oxygen atoms from water molecules. At basic pH values a [Cu(L)H(-3)](-) species with a pseudo-octahedral geometry was also obtained, with four nitrogen donor atoms in its equatorial plane, coming from the histidine residue and from peptidic nitrogen atoms. Interestingly, at pH values relatively higher than the neutrality, the coordination sphere of the copper complex in the [Cu(L)H(-2)] species changes its stereochemistry towards a pseudo-octahedron, as suggested by the change in the parallel copper hyperfine coupling constant of the EPR spectra at low temperature. A slight difference in the redox potentials between this two-faced [Cu(L)H(-2)] complex species seems to confirm this behaviour. Both potentiometric and spectroscopic data were compared with the analogous species obtained with the Ac-PHGGGWGQ-NH(2) peptide, belonging to the octarepeat domain of the human prion protein (hPrP) N-terminal region. The [Cu(L)H(-2)] species formed by the Ac-PHPGGSNWGQ-NH(2) decapeptide, having a slightly lower stability, turned out to be less abundant and to exist within a narrow pH range.
Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein
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Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein
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View Export to BibTeX Export to EndNote
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Impact Factor: 3.838
View Export to BibTeX Export to EndNote
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Impact Factor: 5.925
View Export to BibTeX Export to EndNote
Tabbì G, Di Mauro G, Purrello R, Bonomo RP
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Impact Factor: 3.838
View Export to BibTeX Export to EndNote
La Mendola D, Magrì A, Vagliasindi LI, Hansson Ö, Bonomo RP, Rizzarelli E
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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 (583 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
Banyasz A, Karpati S, Mercier Y, Reguero M, Gustavsson T, Markovitsi D, Improta R
* The peculiar spectral properties of amino-substituted uracils: A combined theoretical and experimental study (486 views)
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Impact Factor: 3.603
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 (1287 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
Mazzaglia A, Micali N, Scolaro LM, Attanasio F, Magrí A, Pappalardo G, Villari V
* Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: A comparative study with two PEG-conjugated variants of the human sequence (572 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Jan 21; 114(2): 705-713.
Impact Factor: 3.603
View Export to BibTeX Export to EndNote
Improta R, Santoro F, Barone V, Lami A
* Vibronic model for the quantum dynamical study of the competition between bright and charge-transfer excited states in single-strand polynucleotides: the adenine dimer case (361 views)
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Impact Factor: 2.899
View Export to BibTeX Export to EndNote
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Impact Factor: 2.605
View Export to BibTeX Export to EndNote
Improta R, Barone V, Lami A, Santoro F
* Quantum dynamics of the ultrafast ππ*/nπ* population transfer in uracil and 5-fluoro-uracil in water and acetonitrile (325 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2009 Oct 29; 113(43): 14491-14503.
Impact Factor: 3.471
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 (486 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
Karunakaran V, Kleinermanns K, Improta R, Kovalenko SA
* Photoinduced dynamics of guanosine monophosphate in water from broad-band transient absorption spectroscopy and quantum-chemical calculations (379 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2009; 131(16): 5839-5850.
Impact Factor: 8.58
View Export to BibTeX Export to EndNote
Sgarlata C, Bonaccorso C, Gulino FG, Zito V, Arena G, Sciotto D
* Sterochemistry And Thermodynamics Of The Inclusion Of Aliphatic And Aromatic Anionic Guests In A Tetracationic Calix [4] Arene In Acidic And Neutral Aqueous Solutions (353 views)
New Journal Of Chemistry, 2009; 33: 991-991.
Impact Factor: 3.159
View Export to BibTeX Export to EndNote
Santoro F, Barone V, Improta R
* The Excited States Decay Of The A-T Dna: A Pcm/Td-Dft Study In Aqueous Solution Of The (9-Methyl-Adenine) 2 (1-Methyl-Thymine) 2 Stacked Tetramer (327 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2009; 131(42): 15232-15245.
Impact Factor: 8.58
View Export to BibTeX Export to EndNote
Bonomo RP, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
* Nitrogen oxide interaction with copper complexes formed by small peptides belonging to the prion protein octa-repeat region (694 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2007 Apr 14; (14): 1400-1408.
Impact Factor: 3.212
View Export to BibTeX Export to EndNote
Campagna T, Grasso G, Rizzarelli E, Vecchio G
L- and D-cysteine derivatives of β-cyclodextrin: Different molecular recognition properties of their copper(II) complexes for amino acids (426 views)
Inorg Chim Acta (ISSN: 0020-1693), 1998; 275-276: 395-400.
Impact Factor: 1.454
View Export to BibTeX Export to EndNote
Marletta F, Rizzarelli E, Mangiameli A, Brogna A, Sammartano S, Monaco S, Blasi A
Effects of graded doses of copper complexes of L-aminoacids on gastric acid secretion in rats (1374 views)
Boll Soc Ital Biol Sper (ISSN: 0037-8771), 1979 Apr 30; 55(8): 769-775.
Impact Factor: 0
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25 Records (24 excluding Abstracts).
Total impact factor: 97.281 (94.122 excluding Abstracts).
Total 5 year impact factor: 102 (99.163 excluding Abstracts).
Total impact factor: 97.281 (94.122 excluding Abstracts).
Total 5 year impact factor: 102 (99.163 excluding Abstracts).
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