Copper, BDNF and Its N-terminal domain: inorganic features and biological perspectives (538 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2012 Dec 3; 18(49): 15618-15631.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.831, 5-year impact factor: 5.623
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84870031931&partnerID=40&md5=88ae3add55739ad4a09c2f03b4a9aba9
Keywords: Antiproliferation, Biological Activity, Copper, Peptides, Uv Vis Spectroscopy, After-Treatment, Alzheimer, S Disease, Amino Group, Amino-Terminal Domain, Aspartate Residue, Brain-Derived Neurotrophic Factors, Carboxylate Groups, Metal Addition, Metal Binding, Metal Coordination, N-Terminal Domains, Nerve Growth Factor, Neuroblastoma Cell Lines, Neurodegenerative Disorders, Nitrogen Atom, Parallel Tempering, Pathological Conditions, Peptide Fragments, Peripheral Nervous System, Physiological Ph, Potentiometry, Proliferative Activity, Protein Domains, Recognition Site, Spectroscopic Method, Synaptic Plasticity, Terminal Amino Groups, Amides, Amino Acids, Bioactivity, Carboxylation, Cell Culture, Coordination Reactions, Digital Storage, Enzyme Inhibition, Metal Ions, Ph Effects, Spectroscopic Analysis, Ultraviolet Visible Spectroscopy, Copper Compounds, Brain Derived Neurotrophic Factor, Amino Acid Sequence, Article, Binding Site, Chemistry, Circular Dichroism, Human, Metabolism, Ultraviolet Spectrophotometry, Brain-Derived Neurotrophic Factor Metabolism, Copper Chemistry Metabolism, Nerve Growth Factor Chemistry Metabolism, Peptide Fragments Chemistry Metabolism,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita degli Studi di Catania, Italy.
Scuola Superiore di Catania, Via Vadisavoia 9, 95123 Catania, Italy
Istituto di Biostrutture e Bioimmagini-CNR, Dipartimento di Scienze Chimiche, Viale A. Doria 6, 95125 Catania, Italy
References:
Not available.
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2012 Dec 3; 18(49): 15618-15631.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.831, 5-year impact factor: 5.623
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84870031931&partnerID=40&md5=88ae3add55739ad4a09c2f03b4a9aba9
Keywords: Antiproliferation, Biological Activity, Copper, Peptides, Uv Vis Spectroscopy, After-Treatment, Alzheimer, S Disease, Amino Group, Amino-Terminal Domain, Aspartate Residue, Brain-Derived Neurotrophic Factors, Carboxylate Groups, Metal Addition, Metal Binding, Metal Coordination, N-Terminal Domains, Nerve Growth Factor, Neuroblastoma Cell Lines, Neurodegenerative Disorders, Nitrogen Atom, Parallel Tempering, Pathological Conditions, Peptide Fragments, Peripheral Nervous System, Physiological Ph, Potentiometry, Proliferative Activity, Protein Domains, Recognition Site, Spectroscopic Method, Synaptic Plasticity, Terminal Amino Groups, Amides, Amino Acids, Bioactivity, Carboxylation, Cell Culture, Coordination Reactions, Digital Storage, Enzyme Inhibition, Metal Ions, Ph Effects, Spectroscopic Analysis, Ultraviolet Visible Spectroscopy, Copper Compounds, Brain Derived Neurotrophic Factor, Amino Acid Sequence, Article, Binding Site, Chemistry, Circular Dichroism, Human, Metabolism, Ultraviolet Spectrophotometry, Brain-Derived Neurotrophic Factor Metabolism, Copper Chemistry Metabolism, Nerve Growth Factor Chemistry Metabolism, Peptide Fragments Chemistry Metabolism,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita degli Studi di Catania, Italy.
Scuola Superiore di Catania, Via Vadisavoia 9, 95123 Catania, Italy
Istituto di Biostrutture e Bioimmagini-CNR, Dipartimento di Scienze Chimiche, Viale A. Doria 6, 95125 Catania, Italy
References:
Not available.
Copper, BDNF and Its N-terminal domain: inorganic features and biological perspectives
Brain-derived neurotrophic factor (BDNF) is a neurotrophin that influences development, maintenance, survival, and synaptic plasticity of central and peripheral nervous systems. Altered BDNF signaling is involved in several neurodegenerative disorders including Alzheimer's disease. Metal ions may influence the BDNF activity and it is well known that the alteration of Cu(2+) homeostasis is a prominent factor in the development of neurological pathologies. The N-terminal domain of BDNF represents the recognition site of its specific receptor TrkB, and metal ions interaction with this protein domain may influence the protein/receptor interaction. In spite of this, no data inherent the interaction of BDNF with Cu(2+) ions has been reported up to now. Cu(2+) complexes of the peptide fragment BDNF(1-12) encompassing the sequence 1-12 of N-terminal domain of human BDNF protein were characterized by means of potentiometry, spectroscopic methods (UV/Vis, CD, EPR), parallel tempering simulations and DFT-geometry optimizations. Coordination features of the acetylated form, Ac-BDNF(1-12), were also characterized to understand the involvement of the terminal amino group. Whereas, an analogous peptide, BDNF(1-12)D3N, in which the aspartate residue was substituted by an asparagine, was synthesized to provide evidence on the possible role of carboxylate group in Cu(2+) coordination. The results demonstrated that the amino group is involved in metal binding and the metal coordination environment of the predominant complex species at physiological pH consisted of one amino group, two amide nitrogen atoms, and one carboxylate group. Noteworthy, a strong decrease of the proliferative activity of both BDNF(1-12) and the whole protein on a SHSY5Y neuroblastoma cell line was found after treatment in the presence of Cu(2+). The effect of metal addition is opposite to that observed for the analogous fragment of nerve growth factor (NGF) protein, highlighting the role of specific domains, and suggesting that Cu(2+) may drive different pathways for the BDNF and NGF in physiological as well as pathological conditions. Copyright 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Brain-derived neurotrophic factor (BDNF) is a neurotrophin that influences development, maintenance, survival, and synaptic plasticity of central and peripheral nervous systems. Altered BDNF signaling is involved in several neurodegenerative disorders including Alzheimer's disease. Metal ions may influence the BDNF activity and it is well known that the alteration of Cu(2+) homeostasis is a prominent factor in the development of neurological pathologies. The N-terminal domain of BDNF represents the recognition site of its specific receptor TrkB, and metal ions interaction with this protein domain may influence the protein/receptor interaction. In spite of this, no data inherent the interaction of BDNF with Cu(2+) ions has been reported up to now. Cu(2+) complexes of the peptide fragment BDNF(1-12) encompassing the sequence 1-12 of N-terminal domain of human BDNF protein were characterized by means of potentiometry, spectroscopic methods (UV/Vis, CD, EPR), parallel tempering simulations and DFT-geometry optimizations. Coordination features of the acetylated form, Ac-BDNF(1-12), were also characterized to understand the involvement of the terminal amino group. Whereas, an analogous peptide, BDNF(1-12)D3N, in which the aspartate residue was substituted by an asparagine, was synthesized to provide evidence on the possible role of carboxylate group in Cu(2+) coordination. The results demonstrated that the amino group is involved in metal binding and the metal coordination environment of the predominant complex species at physiological pH consisted of one amino group, two amide nitrogen atoms, and one carboxylate group. Noteworthy, a strong decrease of the proliferative activity of both BDNF(1-12) and the whole protein on a SHSY5Y neuroblastoma cell line was found after treatment in the presence of Cu(2+). The effect of metal addition is opposite to that observed for the analogous fragment of nerve growth factor (NGF) protein, highlighting the role of specific domains, and suggesting that Cu(2+) may drive different pathways for the BDNF and NGF in physiological as well as pathological conditions. Copyright 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Copper, BDNF and Its N-terminal domain: inorganic features and biological perspectives
Copper, BDNF and Its N-terminal domain: inorganic features and biological perspectives
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Diana D, Basile A, De Rosa L, Di Stasi R, Auriemma S, Arra C, Pedone C, Turco MC, Fattorusso R, D'Andrea LD
* Beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (vegf) Receptors: Design, Nmr Characterization, And Biological Activity (632 views)
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2011 Dec 2; 286(48): 41680-41691.
Impact Factor: 4.773
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Milite C, Castellano S, Benedetti R, Tosco A, Ciliberti C, Vicidomini C, Boully L, Franci G, Altucci L, Mai A, Sbardella G
* Modulation of the activity of histone acetyltransferases by long chain alkylidenemalonates (LoCAMs) (387 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 1464-3391electronic), 2011 Jun 15; 19(12): 3690-3701.
Impact Factor: 2.921
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Correale S, Pirone L, Di Marcotullio L, De Smaele E, Greco A, Mazzà D, Moretti M, Alterio V, Vitagliano L, Di Gaetano S, Gulino A, Pedone E
* Molecular organization of the cullin E3 ligase adaptor KCTD11 (596 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2011 Apr; 93(4): 715-724.
Impact Factor: 3.022
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Travaglia A, Arena G, Fattorusso R, Isernia C, La Mendola D, Malgieri G, Nicoletti VG, Rizzarelli E
* The inorganic perspective of nerve growth factor: interactions of Cu2+ and Zn2+ with the N-terminus fragment of nerve growth factor encompassing the recognition domain of the TrkA receptor (505 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Mar 21; 17(13): 3726-3738.
Impact Factor: 5.925
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Pizzo E, Merlino A, Turano M, Russo Krauss I, Coscia F, Zanfardino A, Varcamonti M, Furia A, Giancola C, Mazzarella L, Sica F, D'Alessio G
* A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish (884 views)
Biochem J (ISSN: 1470-8728electronic, 0264-6021linking, 0264-6021print), 2011 Jan 15; 433(2): 345-355.
Impact Factor: 4.897
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Pensato S, Saviano M, Bianchi N, Borgatti M, Fabbri E, Gambari R, Romanelli A
* Gamma-Hydroxymethyl Pnas: Synthesis, Interaction With Dna And Inhibition Of Protein/Dna Interactions (392 views)
Bioorg Chem, 2010 Sep; 38(5): 196-201.
Impact Factor: 2.141
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Roviello GN, Di Gaetano S, Capasso D, Cesarani A, Bucci EM, Pedone C
* Synthesis, spectroscopic studies and biological activity of a novel nucleopeptide with Moloney murine leukemia virus reverse transcriptase inhibitory activity (453 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2010 May; 38(5): 1489-1496.
Impact Factor: 4.106
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Roviello GN, Musumeci D, De Cristofaro A, Capasso D, Di Gaetano S, Bucci EM, Pedone C
* Alternate dab-aegPNAs: synthesis, nucleic acid binding studies and biological activity (539 views)
Mol Biosyst (ISSN: 1742-2051, 1742-206x, 1742-2051electronic), 2010 Jan; 6(1): 199-205.
Impact Factor: 3.825
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Arpaia P, Clemente F, Manna C
* In vivo assessment of skin impedance recovery after low-voltage pulses electroporation (5551 views)
Imeko Tc Int Symp (ISSN: 9788-8903), 2008; N/D: 934-937.
Impact Factor: 0
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Improta R, Barone V, Santoro F
* Ab initio calculations of absorption spectra of large molecules in solution: Coumarin C153 (551 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2007; 46(3): 405-408.
Impact Factor: 10.031
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Dalla Bona A, Formaggio F, Peggion C, Kaptein B, Broxterman Quirinus B, Galdiero S, Galdiero M, Vitiello M, Benedetti E, Toniolo C
* Synthesis, conformation, and bioactivity of novel analogues of the antiviral lipopeptide halovir (581 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 748-757.
Impact Factor: 1.801
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Saviano M, Romanelli A, Bucci E, Pedone C, Mischiati C, Bianchi N, Feriotto G, Borgatti M, Gambari R
Computational procedures to explain the different biological activity of DNA/DNA, DNA/PNA and PNA/PNA hybrid molecules mimicking NF-κB binding sites (559 views)
J Biomol Struct Dyn (ISSN: 0739-1102, 1538-0254electronic, 0739-1102linking), 2000 Dec; 18(3): 353-362.
Impact Factor: 1.826
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Caliendo G, Fiorino F, Grieco P, Perissutti E, De Luca S, Giuliano A, Santelli G, Califano D, Severino B, Santagada V
Synthesis and biological activity of pseudopeptides inhibitors of Ras farnesyl transferase containing unconventional amino acids (604 views)
Farmaco (ISSN: 0014-827x), 1999 Nov; 54(11-12): 785-790.
Impact Factor: 0.406
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29 Records (29 excluding Abstracts).
Total impact factor: 117.217 (117.217 excluding Abstracts).
Total 5 year impact factor: 116.602 (116.602 excluding Abstracts).
Total impact factor: 117.217 (117.217 excluding Abstracts).
Total 5 year impact factor: 116.602 (116.602 excluding Abstracts).
538 views. Last view on Thursday 07 December 2023, 20:09:28
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