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10 results on '"Alice Santoro"'

1. Neutralization of Reactive Oxygen Species at Dinuclear Cu(II)-Cores: Tuning the Antioxidant Manifold in Water by Ligand Design

Author

Marco Bortolus, Alice Santoro, Rita De Zorzi, Silvano Geremia, Marcella Bonchio, Marilena Di Valentin, Mauro Carraro, Andrea Squarcina, Neal Hickey, Squarcina, Andrea, Santoro, Alice, Hickey, JAMES NEIL, De Zorzi, R., Carraro, Mauro, Geremia, Silvano, Bortolus, Marco, Di Valentin, Marilena, and Bonchio, Marcella

Subjects
Antioxidant, medicine.medical_treatment, 010402 general chemistry, 01 natural sciences, Medicinal chemistry, Catalysis, Neutralization, antioxidant catalysis, Superoxide dismutase, chemistry.chemical_compound, parasitic diseases, medicine, Phenol, heterocyclic compounds, chemistry.chemical_classification, artificial enzyme, Reactive oxygen species, copper catalysis, biology, 010405 organic chemistry, Chemistry, Ligand, copper catalysi, organic chemicals, catalase, General Chemistry, superoxide dismutase, artificial enzymes, 0104 chemical sciences, artificial enzymes, copper catalysis, superoxide dismutase, catalase, Catalase, biology.protein
Abstract

Dinuclear Cu-2(II,II)-cores stabilized by the N3O donorset of HL1 = (2-{[[di(2-pyridyl)methyl](methyl)amino]methyl}phenol), HL2 = 2-({[di(2-pyridyl)methyl] amino}methyl)phenol), and HL3 = 2-({[di(2-pyridyl)methyl]amino}methyl)-4-nitrophenol display a unique superoxide dismutase (SOD) combined with catalase (CAT)-like activity in water, at neutral pH. The Cu2L21 < Cu2L22 < Cu2L23 structure-reactivity trend puts a spotlight on the electron-deficient core of Cu2L23 that exhibits the highest SOD (log k(cat) (O-2(center dot-)) = 7.55) and CAT-like (k(H2O2) = 0.66 M(-1)s(-1)) performance. Time-lapse ESI-MS and EPR experiments indicate that a dimeric core is essential for oxygenic turnover upon H2O2 decomposition.

Published
2020

2. The Glutathione/Metallothionein System Challenges the Design of Effient O2‐Activating Copper Complexes

Author

Manuel David Peris-Díaz, Peter Faller, Alice Santoro, Gabriele Meloni, Artur Krężel, Jenifer S. Calvo, Institut de Chimie de Strasbourg, Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Departement of Chemistry and Biochemistry, University of Texas at Dallas [Richardson] (UT Dallas), and University of Wrocław [Poland] (UWr)

Subjects
chemistry.chemical_element, Ascorbic Acid, 010402 general chemistry, 01 natural sciences, Redox, Catalysis, Article, 03 medical and health sciences, chemistry.chemical_compound, Metallothionein, [CHIM.COOR]Chemical Sciences/Coordination chemistry, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 030304 developmental biology, 0303 health sciences, 010405 organic chemistry, Bioinorganic chemistry, General Medicine, General Chemistry, Glutathione, Copper, Combinatorial chemistry, 0104 chemical sciences, Oxygen, Cytosol, chemistry, 13. Climate action, Oxidation-Reduction, Intracellular
Abstract

Copper-complexes are of medicinal and biological interest, including as anticancer drugs designed to cleave intracellular biomolecules via O(2) activation. To exhibit such activity, the copper complex must be redox-active and resistant to dissociation. Metallothioneins (MTs) and glutathione (GSH) are abundant in the cytosol and nucleus. Because they also are thiol-rich reducing molecules with high Cu(I)-affinity, they are potential competitors for copper ion bound in a copper drug. Here, we investigated a panel of Cu(I)/ Cu(II)-complexes often used as drugs, from various classes, with diverse coordination chemistries and redox potentials. We evaluated their catalytic activity in ascorbate oxidation based on redox-cycling between Cu(I) and Cu(II), as well as their resistance to dissociation or inactivation under cytosolically-relevant concentrations of GSH and MT. Our findings show that O(2)-activating Cu(I)/ Cu(II)-complexes for cytosolic/nuclear targets are generally not stable against the GSH/MT system, which creates a challenge for their future design.

Published
2020

3. Cu transfer from amyloid-β4–16 to metallothionein-3: the role of the neurotransmitter glutamate and metallothionein-3 Zn(<scp>ii</scp>)-load states

Author

Adam Pomorski, Nina E. Wezynfeld, Ewelina Stefaniak, Artur Krężel, Dawid Płonka, Peter Faller, Wojciech Bal, and Alice Santoro

Subjects
inorganic chemicals, Amyloid, Copper metabolism, chemistry.chemical_element, Zinc, 010402 general chemistry, 01 natural sciences, Catalysis, chemistry.chemical_compound, Materials Chemistry, Neurotransmitter, chemistry.chemical_classification, urogenital system, 010405 organic chemistry, Biomolecule, Metals and Alloys, Glutamate receptor, General Chemistry, Copper, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, chemistry, Biochemistry, Ceramics and Composites, Metallothionein 3
Abstract

Copper transfer from Cu(ii)amyloid-β4-16 to human Zn7-metallothionein-3 can be accelerated by glutamate and by lowering the Zn-load of metallothionein-3 with EDTA. Glutamate facilitates the Cu(ii) release, and Zn4-6-metallothionein-3 react more rapidly. These mechanisms are additive, proving the intricate and interconnected network of zinc and copper trafficking between biomolecules.

Published
2018

4. Cysteine and glutathione trigger the Cu–Zn swap between Cu(<scp>ii</scp>)-amyloid-β4-16peptide and Zn7-metallothionein-3

Author

Alice Santoro, Milan Vašák, Wojciech Bal, Nina E. Wezynfeld, and Peter Faller

Subjects
0301 basic medicine, Amyloid, Stereochemistry, Peptide, Plasma protein binding, 010402 general chemistry, 01 natural sciences, Catalysis, Turn (biochemistry), 03 medical and health sciences, chemistry.chemical_compound, Materials Chemistry, chemistry.chemical_classification, Metals and Alloys, Oxidation reduction, General Chemistry, Glutathione, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, 030104 developmental biology, Biochemistry, chemistry, Ceramics and Composites, Metallothionein 3, Cysteine
Abstract

Cysteine and glutathione are able to reduce Cu(II) coordinated to the peptide amyloidβ4-16, and shuttle the resulting Cu(I) to partially replace Zn(II) in the protein Zn7-metallothionein-3. The released Zn(II) in turn binds to amyloid-β4-16. Thus cysteine and glutathione are modulators of Cu/Zn-distribution between metallothionein-3 and amyloid-β4-16.

Published
2017

5. Reactivity of Cu(ii)-, Zn(ii)- and Fe(ii)-thiosemicarbazone complexes with glutathione and metallothionein: from stability to dissociation to transmetallation

Author

Alice Santoro, Peter Faller, Manuel David Peris-Díaz, Christian Gaiddon, Òscar Palacios, Bertrand Vileno, Gilles Riegel, Artur Krężel, Institut de Chimie de Strasbourg, Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Centre National de la Recherche Scientifique (CNRS)-Université Louis Pasteur - Strasbourg I-Institut de Chimie du CNRS (INC), Institute of Environmental Assessment and Water Research (IDAEA), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), Interface de Recherche Fondamentale et Appliquée en Cancérologie (IRFAC - Inserm U1113), and Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Paul Strauss : Centre Régional de Lutte contre le Cancer (CRLCC)-Fédération de Médecine Translationelle de Strasbourg (FMTS)

Subjects
Thiosemicarbazones, 0301 basic medicine, Iron, Metal ions in aqueous solution, Biophysics, chemistry.chemical_element, Zinc, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, Ligands, Biochemistry, Medicinal chemistry, Dissociation (chemistry), Biomaterials, Metal, 03 medical and health sciences, chemistry.chemical_compound, Transmetalation, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Semicarbazone, ComputingMilieux_MISCELLANEOUS, 030102 biochemistry & molecular biology, Ligand, Metals and Alloys, Hydrogen-Ion Concentration, Glutathione, Copper, 3. Good health, 030104 developmental biology, chemistry, Chemistry (miscellaneous), visual_art, visual_art.visual_art_medium, Metallothionein, Spectrophotometry, Ultraviolet, Chimie/Autre, Reactive Oxygen Species
Abstract

Thiosemicarbazones (TSCs) are a class of strong metal ion ligands, which are currently being investigated for several applications, such as anticancer treatment. In addition to these ligands only, which exert their activity upon interaction with metal ions in cells, preformed metal–TSC complexes are also widely studied, predominantly with the essential metal ions iron, copper and zinc. Currently, it is unclear what the active species are, which complexes are present and what are their biological targets. Herein, we study the complexes of copper(ii), zinc(ii) and iron(ii) with three TSCs, PT, 3-AP (triapine) and Dp44mT, (latter two are currently in clinical trials), concerning their reactivity with glutathione (GSH) and Zn7-metallothionein (Zn7MT-1, 2 and 3). These two cysteine-containing molecules can have a major impact on metal–TSC complexes because they are abundant in the cytosol and nucleus, they are strong metal ligands and have the potential to reduce Cu(ii) and Fe(iii). Our results indicate that Fe(ii)–TSC is stable in the presence of typical cytosolic concentrations of GSH and Zn7MT. In contrast, all three Cu(ii)–TSCs react rapidly due to the reduction of Cu(ii) to Cu(i), which is then transferred to MT. This suggests that Cu(ii)–TSCs are rapidly dissociated in a cytosolic-type environment and the catalytic generation of reactive oxygen species by Cu(ii)–TSCs is stopped. Moreover, in the case Cu(ii)–Dp44mT, transmetallation with Zn(ii) from MT occurs. The reaction of Zn(ii)–TSCs is ligand dependent, from predominant dissociation for PT and 3-AP, to very little dissociation of Zn(ii)–Dp44mT2. These results indicate that GSH and Zn7MT may be important factors in the fate of Cu(ii)– and Zn(ii)–TSCs. In particular, for Cu, its chemistry is complex, and these reactions may also occur for other families of Cu-complexes used in cancer treatment or for other applications.

Published
2019

6. Cu transfer from amyloid-β

Author

Alice, Santoro, Nina Ewa, Wezynfeld, Ewelina, Stefaniak, Adam, Pomorski, Dawid, Płonka, Artur, Krężel, Wojciech, Bal, and Peter, Faller

Subjects
Neurotransmitter Agents, Amyloid beta-Peptides, Organometallic Compounds, Glutamic Acid, Humans, Nerve Tissue Proteins, Copper, Metallothionein 3, Peptide Fragments
Abstract

Copper transfer from Cu(ii)amyloid-β4-16 to human Zn7-metallothionein-3 can be accelerated by glutamate and by lowering the Zn-load of metallothionein-3 with EDTA. Glutamate facilitates the Cu(ii) release, and Zn4-6-metallothionein-3 react more rapidly. These mechanisms are additive, proving the intricate and interconnected network of zinc and copper trafficking between biomolecules.

Published
2018

7. Low catalytic activity of the Cu( ii )-binding motif (Xxx-Zzz-His; ATCUN) in reactive oxygen species production and inhibition by the Cu( i )-chelator BCS

Author

Laurent Raibaut, Gulshan R. Walke, Prasad P. Kulkarni, Alice Santoro, Bertrand Vileno, Peter Faller, Institut de Chimie de Strasbourg, Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), RENARD (TGE Réseau National de RPE interdisciplinaire - 3443), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-FR-CNRS 3443-Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Agharkar Research Institute (ARI), Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), RENARD (TGE Réseau National de RPE interdisciplinaire - 3443 ), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Université de Strasbourg (UNISTRA)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Descartes - Paris 5 (UPD5)-Université de Lille-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Lille-Sorbonne Université (SU)-Aix Marseille Université (AMU)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), and Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS)

Subjects
chemistry.chemical_classification, Reactive oxygen species, 010405 organic chemistry, Chemistry, Biomolecule, Metals and Alloys, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, General Chemistry, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, 010402 general chemistry, 01 natural sciences, Combinatorial chemistry, Catalysis, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Redox Activity, Cytosol, Materials Chemistry, Ceramics and Composites, Chelation, ComputingMilieux_MISCELLANEOUS
Abstract

The catalytic redox activity of Cu(ii) bound to the motif NH2-Xxx-Zzz-His (ATCUN) with ascorbate and H2O2/O2 is very low and can be stopped via Cu(i)-chelation. This impacts its application as an artificial Cu-enzyme to degrade biomolecules via production of reactive oxygen species in a Cu(i)-chelator rich environment like the cytosol.

Published
2018

8. Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance

Author

Elena Atrián-Blasco, Peter Faller, Christelle Hureau, Paulina Gonzalez, Bruno Alies, Alice Santoro, Laboratoire de chimie de coordination (LCC), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie de Strasbourg, Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), ChemBioPharm, Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), European Project: 638712,H2020,ERC-2014-STG,aLzINK(2015), Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, familial mutations, Amyloid β, Amyloid, Amylin, chemistry.chemical_element, Zinc, 010402 general chemistry, 01 natural sciences, Article, Inorganic Chemistry, Type ii diabetes, 03 medical and health sciences, α-synuclein, Materials Chemistry, Amyloid-β, [CHIM.COOR]Chemical Sciences/Coordination chemistry, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Physical and Theoretical Chemistry, Metal binding, Chemistry, zinc, 3. Good health, 0104 chemical sciences, 030104 developmental biology, Biochemistry, copper, α synuclein, amylin
Abstract

International audience; Several diseases share misfolding of different peptides and proteins as a key feature for their development. This is the case of important neurodegenerative diseases such as Alzheimer’s and Parkinson’s diseases and type II diabetes mellitus. Furthermore, metal ions such as copper and zinc might play an important role upon interaction with amyloidogenic peptides and proteins, which could impact their aggregation and toxicity abilities. In this review, the different coordination modes proposed for copper and zinc with amyloid-β, α-synuclein and IAPP will be reviewed as well as their impact on the aggregation, and ROS production in the case of copper. In addition, a special focus will be given to the mutations that affect metal binding and lead to familial cases of the diseases. Different modifications of the peptides that have been observed in vivo and could be relevant for the coordination of metal ions are also described.

Published
2018
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9. Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins

Author

Christelle Hureau, Peter Faller, Elena Atrián-Blasco, Dean Louis Pountney, Alice Santoro, Gabriele Meloni, Laboratoire de chimie de coordination (LCC), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Fédérale Toulouse Midi-Pyrénées, Université Toulouse III - Paul Sabatier (UT3), Institut de Chimie de Strasbourg, Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Menzies Health Institute Queensland, Griffith University [Brisbane], Departement of Chemistry and Biochemistry, University of Texas at Dallas [Richardson] (UT Dallas), Institute for Advanced Study (USIAS), European Project: 638712,H2020,ERC-2014-STG,aLzINK(2015), Institut de Chimie de Toulouse (ICT), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT), Institut d’Etudes Avancées de l’Université de Strasbourg - Institute for Advanced Study (USIAS), Université de Strasbourg (UNISTRA), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

Subjects
0301 basic medicine, chemistry.chemical_classification, Reactive oxygen species, Chemistry, Context (language use), Amyloidogenic Proteins, General Chemistry, Metabolism, medicine.disease_cause, Article, 3. Good health, Coordination complex, 03 medical and health sciences, 030104 developmental biology, Biochemistry, medicine, Gene silencing, Metallothionein, Animals, Humans, [CHIM.COOR]Chemical Sciences/Coordination chemistry, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Oxidative stress, Cysteine
Abstract

International audience; Cu and Zn ions are essential in most living beings. Their metabolism is critical for health and mis-metabolism can be lethal. In the last two decades, a large body of evidence has reported the role copper, zinc and iron, and oxidative stress in several neurodegenerative diseases like Alzheimer, Parkinson, Prion, etc. To what extend this mis-metabolism is causative or a consequence of these diseases is still a matter of research. In this context metallothioneins (MTs) appear to play a central gate-keeper role in controlling aberrant metal-protein interactions. MTs are small proteins that can bind high amounts of Zn(II) and Cu(I) ions in metal-cluster arrangements via their cysteines thiolates. Moreover, MTs are well known antioxidants. The present tutorial outlines the chemistry underlying the interconnection between copper(I/II) and zinc(II) coordination to amyloidogenic proteins and MTs, and their redox properties in generation and/or silencing reactive oxygen species (overproduced in oxidative stress) and other reactants. These studies have revealed the coordination chemistry involved in neurodegenerative diseases and the interactions between MTs with amyloidogenic proteins metal-complexes (like amyloid-β, α-synuclein and prion-protein). Overall, a protective role of MTs in neurodegenerative processes is emerging, serving as a foundation for exploring MTs chemistry as inspiration for therapeutic approaches.

Published
2017

10. Cysteine and glutathione trigger the Cu-Zn swap between Cu(ii)-amyloid-β

Author

Alice, Santoro, Nina, Ewa Wezynfeld, Milan, Vašák, Wojciech, Bal, and Peter, Faller

Subjects
Amyloid, Zinc, Amyloid beta-Peptides, Nerve Tissue Proteins, Cysteine, Glutathione, Oxidation-Reduction, Copper, Metallothionein 3, Peptide Fragments, Protein Binding
Abstract

Cysteine and glutathione are able to reduce Cu(ii) coordinated to the peptide amyloidβ

Published
2017

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