Copper(I) and Copper(II) Inhibit A beta Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease (584 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Feb 25; 17(9): 2752-2762.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79951786420&partnerID=40&md5=67a00463edef545d46da93e7514bdafb
Keywords: Copper, Ide, Metalloenzymes, Zinc, Alzheimer, S Disease, Bio-Molecular, Computational Investigation, Copper (ii), Enzymatic Activities, Inhibitory Effect, Insulin-Degrading Enzymes, Kinetic Study, Metal Homeostasis, Metallo-Protease, Molecular Basis, Monovalent Cations, Normal Condition, Peptide Fragments, Substrate Modifications, Degradation, Enzyme Activity, Enzyme Inhibition, Integrodifferential Equations, Mass Spectrometry, Metal Ions, Neurodegenerative Diseases, Zinc Compounds, Aluminum, Amyloid Beta Protein, Cysteine, Insulinase, Silver, Algorithm, Alzheimer Disease, Article, Chemistry, Computer Simulation, Drug Effect, Genetics, Human, Metabolism, Pathology, Sequence Homology, Amyloid Beta-Peptides, Insulysin, Amino Acid,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita di Catania, Catania, Italy.
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, 95125, Catania, Italy
Consorzio I. N. B. B., Viale delle Medaglie d'Oro 305, 00136, Roma, Italy
Department of Experimental Medicine and Biochemical Sciences, University of Roma Tor Vergata, Via Montpellier 1, 00133 Roma, Italy
Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems, Via C. Ulpiani 27, 70126 Bari, Italy
References:
Not available.
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Feb 25; 17(9): 2752-2762.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79951786420&partnerID=40&md5=67a00463edef545d46da93e7514bdafb
Keywords: Copper, Ide, Metalloenzymes, Zinc, Alzheimer, S Disease, Bio-Molecular, Computational Investigation, Copper (ii), Enzymatic Activities, Inhibitory Effect, Insulin-Degrading Enzymes, Kinetic Study, Metal Homeostasis, Metallo-Protease, Molecular Basis, Monovalent Cations, Normal Condition, Peptide Fragments, Substrate Modifications, Degradation, Enzyme Activity, Enzyme Inhibition, Integrodifferential Equations, Mass Spectrometry, Metal Ions, Neurodegenerative Diseases, Zinc Compounds, Aluminum, Amyloid Beta Protein, Cysteine, Insulinase, Silver, Algorithm, Alzheimer Disease, Article, Chemistry, Computer Simulation, Drug Effect, Genetics, Human, Metabolism, Pathology, Sequence Homology, Amyloid Beta-Peptides, Insulysin, Amino Acid,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita di Catania, Catania, Italy.
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, 95125, Catania, Italy
Consorzio I. N. B. B., Viale delle Medaglie d'Oro 305, 00136, Roma, Italy
Department of Experimental Medicine and Biochemical Sciences, University of Roma Tor Vergata, Via Montpellier 1, 00133 Roma, Italy
Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems, Via C. Ulpiani 27, 70126 Bari, Italy
References:
Not available.
Copper(I) and Copper(II) Inhibit A beta Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease
Accumulation of neurotoxic amyloid-beta peptide (Abeta) and alteration of metal homeostasis (metallostasis) in the brain are two main factors that have been very often associated with neurodegenerative diseases, such as Alzheimer's disease (AD). Abeta is constantly produced from the amyloidprecursor-protein APP precursor and immediately catabolized under normal conditions, whereas dysmetabolism of Abeta and/or metal ions seems to lead to a pathological deposition. Although insulin-degrading enzyme (IDE) is the main metalloprotease involved in Abeta degradation in the brain being up-regulated in some areas of AD brains, the role of IDE for the onset and development of AD is far from being understood. Moreover, the biomolecular mechanisms involved in the recognition and interaction between IDE and its substrates are still obscure. In spite of the important role of metals (such as copper, aluminum, and zinc), which has brought us to propose a "metal hypothesis of AD", a targeted study of the effect of metallostasis on IDE activity has never been carried out. In this work, we have investigated the role that various metal ions (i. e., Cu (2+), Cu (+), Zn (2+), Ag (+), and Al (3+)) play in modulating the interaction between IDE and two Abeta peptide fragments, namely Abeta (1-16) and Abeta (16-28). It was therefore possible to identify the direct effect that such metal ions have on IDE structure and enzymatic activity without interferences caused by metal-induced substrate modifications. Mass spectrometry and kinetic studies revealed that, among all the metal ions tested, only Cu (2+), Cu (+), and Ag (+) have an inhibitory effect on IDE activity. Moreover, the inhibition of copper (II) is reversed by adding zinc (II), whereas the monovalent cations affect the enzyme activity irreversibly. The molecular basis of their action on the enzyme is also discussed on the basis of computational investigations. Copyright 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Accumulation of neurotoxic amyloid-beta peptide (Abeta) and alteration of metal homeostasis (metallostasis) in the brain are two main factors that have been very often associated with neurodegenerative diseases, such as Alzheimer's disease (AD). Abeta is constantly produced from the amyloidprecursor-protein APP precursor and immediately catabolized under normal conditions, whereas dysmetabolism of Abeta and/or metal ions seems to lead to a pathological deposition. Although insulin-degrading enzyme (IDE) is the main metalloprotease involved in Abeta degradation in the brain being up-regulated in some areas of AD brains, the role of IDE for the onset and development of AD is far from being understood. Moreover, the biomolecular mechanisms involved in the recognition and interaction between IDE and its substrates are still obscure. In spite of the important role of metals (such as copper, aluminum, and zinc), which has brought us to propose a "metal hypothesis of AD", a targeted study of the effect of metallostasis on IDE activity has never been carried out. In this work, we have investigated the role that various metal ions (i. e., Cu (2+), Cu (+), Zn (2+), Ag (+), and Al (3+)) play in modulating the interaction between IDE and two Abeta peptide fragments, namely Abeta (1-16) and Abeta (16-28). It was therefore possible to identify the direct effect that such metal ions have on IDE structure and enzymatic activity without interferences caused by metal-induced substrate modifications. Mass spectrometry and kinetic studies revealed that, among all the metal ions tested, only Cu (2+), Cu (+), and Ag (+) have an inhibitory effect on IDE activity. Moreover, the inhibition of copper (II) is reversed by adding zinc (II), whereas the monovalent cations affect the enzyme activity irreversibly. The molecular basis of their action on the enzyme is also discussed on the basis of computational investigations. Copyright 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Copper(I) and Copper(II) Inhibit A beta Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease
Copper(I) and Copper(II) Inhibit A beta Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease
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View Export to BibTeX Export to EndNote
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Impact Factor: 13.7
View Export to BibTeX Export to EndNote
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* The zinc - but not cadmium - containing zeta-carbonic from the diatom Thalassiosira weissflogii is potently activated by amines and amino acids (288 views)
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Impact Factor: 3.929
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 4.293
View Export to BibTeX Export to EndNote
Roviello GN, Vicidomini C, Di Gaetano S, Capasso D, Musumeci D, Roviello V
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View Export to BibTeX Export to EndNote
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Impact Factor: 2.686
View Export to BibTeX Export to EndNote
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Impact Factor: 4.882
View Export to BibTeX Export to EndNote
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* The Copper (ii) And Zinc (ii) Coordination Mode Of Hexxh And Hxxeh Motif In Small Peptides: The Role Of Carboxylate Location And Hydrogen Bonding Network (541 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2014 Jan; 130(1): 92-102.
Impact Factor: 3.444
View Export to BibTeX Export to EndNote
Turi I, DSanna D, Garribba E, Pappalardo G, Sóvágó I
* The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine (428 views)
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Impact Factor: 2.047
View Export to BibTeX Export to EndNote
Jószai V, Turi I, Kállay C, Pappalardo G, Di Natale G, Rizzarelli E, Sóvágó I
* Mixed metal copper(II)-nickel(II) and copper(II)-zinc(II) complexes of multihistidine peptide fragments of human prion protein (485 views)
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Impact Factor: 3.197
View Export to BibTeX Export to EndNote
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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 (554 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Sep 16; 17(34): 9448-9455.
Impact Factor: 5.925
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Lanza V, Bellia F, D'Agata R, Grasso G, Rizzarelli E, Vecchio G
* New glycoside derivatives of carnosine and analogs resistant to carnosinase hydrolysis: synthesis and characterization of their copper(II) complexes (434 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2011 Feb; 105(2): 181-188.
Impact Factor: 3.354
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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 (449 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2010 Nov 28; 39(44): 10678-10684.
Impact Factor: 3.647
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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 (504 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
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Di Natale G, Pappalardo G, Milardi D, Sciacca MFM, Attanasio F, La Mendola D, Rizzarelli E
* Different Interactions Of Human And Avian Prion Proteins N-Terminal Tandem Repeat Peptides And Their Copper (ii) Complexes With Model Membranes (385 views)
Journal Of Chemical Physics, 2010; 114: 13830-13838.
Impact Factor: 2.028
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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 (489 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010; 39(30): 7046-7053.
Impact Factor: 3.647
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Di Natale G, Osz K, Nagy Z, Sanna D, Micera G, Pappalardo G, Sovago I, Rizzarelli E
* The Interaction Of Copper (ii) With The Prion Peptide Fragment Huprp (76-114) Encompassing Four Histidyl Residues Within And Outside The Octarepeat Domain (498 views)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2009 May 4; 48(9): 4239-4250.
Impact Factor: 4.657
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Di Natale G, Damante CA, Nagy Z, Osz K, Pappalardo G, Rizzarelli E, Sóvágó I
* Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation (463 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2008 Nov; 102(11): 2012-2019.
Impact Factor: 3.133
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Damante CA, Ösz K, Nagy Z, Pappalardo G, Grasso G, Impellizzeri G, Rizzarelli E, Sóvágó I
* The Metal Loading Ability Of Beta-Amyloid N-Terminus: A Combined Potentiometric And Spectroscopic Study Of Copper (ii) Complexes With Beta-Amyloid (1-16), Its Short Or Mutated Peptide Fragments, And Its Polyethylene Glycol (peg)-Ylated Analogue (591 views)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2008 Oct 20; 47(20): 9669-9683.
Impact Factor: 4.147
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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 (315 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2008 Sep 7; (29): 3805-3816.
Impact Factor: 3.58
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Pappalardo M, Sciacca MFM, Milardi D, Grasso DM, La Rosa C
* Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (333 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581.
Impact Factor: 1.63
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Bellia F, La Mendola D, Maccarrone G, Mineo P, Vitalini D, Scamporrino E, Sortino S, Vecchio G, Rizzarelli E
* Copper(II) Complexes With Beta-Cyclodextrin-Homocarnosine Conjugates And Their Antioxidant Activity (290 views)
Inorg Chim Acta (ISSN: 0020-1693), 2007 Feb 15; 360(3): 945-954.
Impact Factor: 1.713
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La Mendola D, Bonomo RP, Impellizzeri G, Maccarrone G, Pappalardo G, Pietropaolo A, Rizzarelli E, Zito V
* Copper(II) complexes with chicken prion repeats: Influence of proline and tyrosine residues on the coordination features (315 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2005 Sep; 10(5): 463-475.
Impact Factor: 3.224
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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 (351 views)
And Life Sciencesjournal Of Chromatography B Analytical Technologies In The Biomedical, 2004 Feb 5; 800(1-2): 127-133.
Impact Factor: 1.403
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Mineo P, Vitalini D, La Mendola D, Rizzarelli E, Scamporrino E, Vecchio G
* Coordination Features Of Difunctionalized Beta-Cyclodextrins With Carnosine: Esi-Ms And Spectroscopic Investigations On 6a, 6d-Di-(beta-Alanyl-L-Histidine)-6a, 6d-Dideoxy-Beta-Cyclodextrin And 6a, 6c-Di-(beta-Alanyl-L-Histidine)-6a, 6c-Dideoxy-Beta-Cyclodextrin And Their Copper (ii) Complexes (535 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2004 Feb; 98(2): 254-265.
Impact Factor: 2.225
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De Luca S, Bruno G, Fattorusso R, Isernia C, Pedone C, Morelli G
New synthetic tools for peptide-tetraphenylporphyrin derivatives (326 views)
Int J Pept Res Ther (ISSN: 0929-5666, 1573-3149), 1998 Jul; 5(4): 269-276.
Impact Factor: 0.557
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Tabbì G, Nauser T, Koppenol WH, Reedijk J
A Pulse Radiolysis Study of an Imidazolato-Bridged Asymmetric Dicopper(II) Complex: A Structural and Functional Mimic of Superoxide Dismutase (287 views)
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 1998; (12): 1939-1943.
Impact Factor: 2.222
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Bonomo RP, Cucinotta V, D'Alessandro F, Impellizzeri G, Maccarrone G, Rizzarelli E, Vecchio G, Carima L, Corradini R, Sartor G, Marchelli R
Chiral recognition by the copper(ii) complex of 6-deoxy-6-n-(2 - methylaminopyridine)-β-cyclodextrin (399 views)
Chirality (ISSN: 0899-0042), 1997; 9(4): 341-349.
Impact Factor: 1.915
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Pirro F, La Gatta S, Arrigoni F, Famulari A, Maglio O, Vecchio PD, Chiesa M, De Gioia L, Bertini L, Chino M, Nastri F, Lombardi A
* A De Novo‐Designed Type 3 Copper Protein Tunes Catechol Substrate Recognition and Reactivity (6 views)
Angewandte Chemie International Edition, 2023/1/2; 62: e202211552-N/D.
Impact Factor: 16.823
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33 Records (33 excluding Abstracts).
Total impact factor: 161.492 (161.492 excluding Abstracts).
Total 5 year impact factor: 144.576 (144.576 excluding Abstracts).
Total impact factor: 161.492 (161.492 excluding Abstracts).
Total 5 year impact factor: 144.576 (144.576 excluding Abstracts).
584 views. Last view on Thursday 24 August 2023, 14:32:18
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