Copper-related diseases: From chemistry to molecular pathology

Crisponi, Guido; Nurchi, Valeria Marina; Fanni, Daniela; Gerosa, Clara; Nemolato, Sonia; Faa, Gavino

doi:10.1016/j.ccr.2009.12.018

Cited by 217 publications

(107 citation statements)

References 250 publications

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“…Their complex-forming capacity has been utilized in medicine for the treatment of Wilson's disease, for the removal of excess of copper from the liver, and in the prevention of its accumulation [1][2][3][4][5][6][7]. In this paper, we present the affinities of two peptides derived from the N-terminal part of the FBP28 protein (PDB code: 1E0L) to copper (Cu 2?…”

Section: Introductionmentioning

confidence: 99%

Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

Makowska

Wyrzykowski

Hirniak

et al. 2015

J Therm Anal Calorim

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Isothermal titration calorimetry (ITC) was used to study the interactions between copper(II) ions and peptides with sequences taken from the N-terminal loop of the FBP28 protein (formin-binding protein) WW domain: AcLys-Thr-Ala-Asp-Gly-Lys-Thr-NH 2 (D7) and Ac-Tyr-LysThr-Ala-Asn-Gly-Lys-Thr-Tyr-NH 2 (D9 M), respectively. Measurements were taken at 298.15 K in 20 mM 2-(Nmorpholino)ethanesulfonic acid buffer solution at a pH of 6. The stoichiometry, conditional stability constants and thermodynamic parameters (D ITC G, D ITC H and D ITC S) for the pertinent complexation reactions were determined. Furthermore, the thermal stability of peptide conformations in the presence and absence of copper(II) in the system was investigated using differential scanning calorimetry. Finally, a general procedure on how to include the effect of buffer competition with the peptide for the metal as well as proton competition with the metal for the peptide and the buffer's component during ITC data analysis is described.

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Section: Introductionmentioning

confidence: 99%

Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

Makowska

Wyrzykowski

Hirniak

et al. 2015

J Therm Anal Calorim

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“…[1][2][3][4][5] In particular, the involvement of copper in human disease has been described from a both biochemical and a medicinal view. [5][6][7] Studies have concentrated on the biochemical action of Cu(II) complexes with non-steroidal anti-inflammatory drugs, [8] the potential chemotherapeutic properties of Cu-based compounds, [9,10] and the antiviral and antibacterial activity of Cu(II) complexes. [11][12][13] The Cu(II) complexes, exhibiting cytotoxic activity through cell apoptosis or enzyme inhibition, have also been reviewed.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and spectroscopic characterizations of Cu(II) complexes with novel 15‐membered N₄ macrocyclic ligand and their utility to obtain CuO nanostructures for efficient degradation of dyes

Adam

Alhadhrami

Saad

et al. 2017

Applied Organom Chemis

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This paper describes synthesis, characterization and application of a series of Cu(II) complexes with a novel 3-thioxo-[1,2,4,5]tetrazocane-6,8-dione (N 4 ) macrocyclic ligand. The complexes were characterized by physicochemical and spectroscopic techniques, such as UV-visible and IR spectroscopies, molar conductance, magnetic susceptibility measurements, and elemental analysis.The data suggest that the mononuclear Cu(II) complexes have a metal-to-ligand mole ratio of 1:1 and that the Cu(II) ions are coordinated with the four nitrogen atoms inside the N 4 macrocyclic ring. The experimental anisotropic g-values indicate that the chloro, nitrato, acetate, and perchlorato complexes have sixcoordinate distorted octahedral behavior, whereas the sulfato complex has five-coordinate square-pyramidal geometry. A simple and nontoxic method for preparation of CuO nanoparticles based upon the thermal decomposition of the synthesized Cu(II) complexes has been explored. Finally, the degradation of Rhodamine 6G dye by the catalytic performance of nano-sized CuO material has been evaluated.

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“…Likewise, acrodermatitis enteropathica, while less well-studied at a mechanistic level, is caused by a mutation of the SLC39A4 zinc transporter gene (5). Wilson's disease results in copper accumulation, which is known to cause tissue damage due to the generation of reactive oxygen species (4). Similarly, copper and zinc are known to be involved in neurodegenerative diseases, such as Alzheimer's and Parkinson's, again with a connection to oxidative stress, although their precise roles are still unclear (6).…”

mentioning

confidence: 99%

“…For example, Wilson's disease and Menkes disease are two human diseases caused by mutations in copper transporters (4). Likewise, acrodermatitis enteropathica, while less well-studied at a mechanistic level, is caused by a mutation of the SLC39A4 zinc transporter gene (5).…”

mentioning

confidence: 99%

Novel Metal Cation Resistance Systems from Mutant Fitness Analysis of Denitrifying Pseudomonas stutzeri

Vaccaro

Lancaster

Thorgersen

et al. 2016

Appl Environ Microbiol

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Metal ion transport systems have been studied extensively, but the specificity of a given transporter is often unclear from amino acid sequence data alone. In this study, predicted Cu 2؉ IMPORTANCEIn this study, genome-wide mutant fitness data in P. stutzeri RCH2 combined with regulon predictions identify several proteins of unknown function that are involved in resisting zinc and copper toxicity. For zinc, these include a member of the UPF0016 protein family that was previously implicated in Ca 2؉ /H ؉ antiport and a human congenital glycosylation disorder, CorB and CorC, which were previously linked to Mg 2؉ transport, and Psest_3322 and Psest_0618, two proteins with no characterized homologs. Experiments using mutants lacking Psest_3226, Psest_3322, corB, corC, or czcI verified their proposed functions, which will enable future studies of these little-characterized zinc resistance determinants. Likewise, Psest_2850, annotated as an ion antiporter subunit, and the conserved hypothetical protein Psest_0584 are implicated in copper resistance. Physiological connections between previous studies and phenotypes presented here are discussed. Functional and mechanistic understanding of transport proteins improves the understanding of systems in which members of the same protein family, including those in humans, can have different functions.T he responses of microorganisms to metal toxicity have been well studied (1). In brief, metal ions can be toxic by binding to essential proteins or other molecules, causing them to become nonfunctional or function incorrectly. This occurs, for example, where the toxic metal ion binds to a binding site that requires a different metal ion to function. Toxic metal ions can also catalyze reactions that are detrimental to the cell, such as hydroxyl radical generation catalyzed by free iron (Fe 3ϩ/2ϩ ) (2) or iron-sulfur cluster degradation by copper (3).Understanding modes of toxicity and metal resistance systems is important, as the information gained from bacteria can be applied to human physiology and medicine. For example, Wilson's disease and Menkes disease are two human diseases caused by mutations in copper transporters (4). Likewise, acrodermatitis enteropathica, while less well-studied at a mechanistic level, is caused by a mutation of the SLC39A4 zinc transporter gene (5). Wilson's disease results in copper accumulation, which is known to cause tissue damage due to the generation of reactive oxygen species (4). Similarly, copper and zinc are known to be involved in neurodegenerative diseases, such as Alzheimer's and Parkinson's, again with a connection to oxidative stress, although their precise roles are still unclear (6). In addition, copper has long been used as

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Copper-related diseases: From chemistry to molecular pathology

Cited by 217 publications

References 250 publications

Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

Synthesis and spectroscopic characterizations of Cu(II) complexes with novel 15‐membered N₄ macrocyclic ligand and their utility to obtain CuO nanostructures for efficient degradation of dyes

Novel Metal Cation Resistance Systems from Mutant Fitness Analysis of Denitrifying Pseudomonas stutzeri

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Copper-related diseases: From chemistry to molecular pathology

Cited by 217 publications

References 250 publications

Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

Synthesis and spectroscopic characterizations of Cu(II) complexes with novel 15‐membered N4 macrocyclic ligand and their utility to obtain CuO nanostructures for efficient degradation of dyes

Novel Metal Cation Resistance Systems from Mutant Fitness Analysis of Denitrifying Pseudomonas stutzeri

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Synthesis and spectroscopic characterizations of Cu(II) complexes with novel 15‐membered N₄ macrocyclic ligand and their utility to obtain CuO nanostructures for efficient degradation of dyes