Ascorbate Oxidation by Cu(Amyloid-β) Complexes: Determination of the Intrinsic Rate as a Function of Alterations in the Peptide Sequence Revealing Key Residues for Reactive Oxygen Species Production
Open accessAbstract
Along with aggregation of the amyloid-β (Aβ) peptide and subsequent deposit of amyloid plaques, oxidative stress is an important feature in Alzheimer's disease. Cu bound to Aβ is able to produce reactive oxygen species (ROS) by the successive reductions of molecular dioxygen, and the ROS produced contribute to oxidative stress. In vitro, ascorbate consumption parallels ROS production, where ascorbate is the reductant that fuels the reactions. Because the affinity of Cu for Aβ is moderate compared to other biomolecules, the rate of ascorbate consumption is a combination of two contributions. The first one is due to peptide-unbound Cu and the second one to peptide-bound Cu complexes. In the present Article, we aim to determine the amounts of the second contribution in the global ascorbate consumption process. It is defined as the intrinsic rate of ascorbate oxidation, which mathematically corresponds to the rate at an infinite peptide to Cu ratio, i.e., without any contribution from peptide-unbound Cu. We show that, for the wild-type Cu(Aβ) complex, this value equals 10% of the value obtained for peptide-unbound Cu and that this value is strongly dependent on peptide alterations. By examination of the dependence of the intrinsic rate of ascorbate oxidation, followed by UV-vis spectroscopy, for several altered peptides, we determine some of the key residues that influence ROS production.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Oxidative stress and the amyloid beta peptide in Alzheimer’s disease
Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185 · see citing works
Self-citationCopper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M. F., Kieber‐Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,763 · see citing works
Mechanisms for copper acquisition, distribution and regulation
Kim, B., Nevitt, T., & Thiele, D. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.72 · Cited by 1,598 · see citing works
Structure and Spectroscopy of Copper−Dioxygen Complexes
Mirica, L. M., Ottenwaelder, X., & Stack, T. D. P. (2004) · Chemical Reviews · doi:10.1021/cr020632z · Cited by 1,341 · see citing works
Metals, oxidative stress and neurodegenerative disorders
Jomová, K., Vondráková, D., Lawson, M. K., & Valko, M. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0563-x · Cited by 1,053 · see citing works
Structure and mechanism of copper, zinc superoxide dismutase
Tainer, J. A., Getzoff, E. D., Richardson, J. S., & Richardson, D. C. (1983) · Nature · doi:10.1038/306284a0 · Cited by 967 · see citing works
Robinson, N. J., & Winge, D. R. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143539 · Cited by 708 · see citing works
Biological metals and metal-targeting compounds in major neurodegenerative diseases
Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497 · see citing works
Copper in the brain and Alzheimer’s disease
Hung, Y. H., Bush, A. I., & Cherny, R. A. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0600-y · Cited by 496 · see citing works
Adman, E. T. (1991) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60536-7 · Cited by 485 · see citing works
CYTOCHROME C OXIDASE: Structure and Spectroscopy
Michel, H., Behr, J., Harrenga, A., & Kannt, A. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.329 · Cited by 449 · see citing works
Copper, zinc and iron in neurodegenerative diseases (Alzheimer's, Parkinson's and prion diseases)
Kozłowski, H., Łuczkowski, M., Remelli, M., & Valensin, D. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.013 · Cited by 438 · see citing works
Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function
Rubino, J. T., & Franz, K. J. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.11.024 · Cited by 369 · see citing works
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288 · see citing works
Faller, P., Hureau, C., & Penna, G. L. (2014) · Accounts of Chemical Research · doi:10.1021/ar400293h · Cited by 271 · see citing works
Self-citationHureau, C., & Faller, P. (2009) · Biochimie · doi:10.1016/j.biochi.2009.03.013 · Cited by 259 · see citing works
Self-citation&NA; (1945) · The American Journal of the Medical Sciences · doi:10.1097/00000441-194503000-00020 · Cited by 235 · see citing works
Brewer, G. J., Askari, F. K., Dick, R. B., Sitterly, J., Fink, J. K., Carlson, M. D., Kluin, K. J., & Lorincz, M. T. (2009) · Translational research · doi:10.1016/j.trsl.2009.05.002 · Cited by 191 · see citing works
Shearer, J., & Szalai, V. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805940m · Cited by 189 · see citing works
Hureau, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.037 · Cited by 178 · see citing works
Self-citationCu(II) Affinity for the Alzheimer’s Peptide: Tyrosine Fluorescence Studies Revisited
Aliès, B., Renaglia, E., Rózga, M., Bal, W., Faller, P., & Hureau, C. (2012) · Analytical Chemistry · doi:10.1021/ac302629u · Cited by 172 · see citing works
Self-citationAtrián‐Blasco, E., Gonzalez, P., Santoro, A., Aliès, B., Faller, P., & Hureau, C. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.007 · Cited by 168 · see citing works
Self-citationCarboni, E., & Lingor, P. (2015) · Metallomics · doi:10.1039/c4mt00339j · Cited by 167 · see citing works
Delangle, P., & Mintz, E. (2012) · Dalton Transactions · doi:10.1039/c2dt12188c · Cited by 139 · see citing works
Zawisza, I. A., Rózga, M., & Bal, W. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.012 · Cited by 138 · see citing works
Hureau, C., Coppel, Y., Dorlet, P., Solari, P. L., Sayen, S., Guillon, E., Sabater, L., & Faller, P. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904512 · Cited by 137 · see citing works
Self-citationHureau, C., Balland, V., Coppel, Y., Solari, P. L., Fonda, E., & Faller, P. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0570-0 · Cited by 134 · see citing works
Self-citationBioinorganic chemistry of copper coordination to alpha-synuclein: Relevance to Parkinson's disease
Binolfi, A., Quintanar, L., Bertoncini, C. W., Griesinger, C., & Fernández, C. O. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.004 · Cited by 132 · see citing works
Cheignon, C., Jones, M., Atrián-Blasco, E., Kieffer, I., Faller, P., Collin, F., & Hureau, C. (2017) · Chemical Science · doi:10.1039/c7sc00809k · Cited by 132 · see citing works
Self-citationCassagnes, L., Hervé, V., Nepveu, F., Hureau, C., Faller, P., & Collin, F. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201305372 · Cited by 129 · see citing works
Self-citationBinolfi, A., Rodríguez, E. E., Valensin, D., D’Amelio, N., Ippoliti, E., Obal, G., Durán, R., Magistrato, A., Pritsch, O., Zweckstetter, M., et al. (2010) · Inorganic Chemistry · doi:10.1021/ic1016752 · Cited by 128 · see citing works
Balland, V., Hureau, C., & Savéant, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011315107 · Cited by 124 · see citing works
Self-citationNadal, R. C., Rigby, S. E. J., & Viles, J. H. (2008) · Biochemistry · doi:10.1021/bi8011093 · Cited by 118 · see citing works
Aliès, B., Badei, B., Faller, P., & Hureau, C. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201102746 · Cited by 99 · see citing works
Self-citationMutual interference of Cu and Zn ions in Alzheimer's disease: perspectives at the molecular level
Atrián‐Blasco, E., Conte‐Daban, A., & Hureau, C. (2017) · Dalton Transactions · doi:10.1039/c7dt01344b · Cited by 96 · see citing works
Self-citationExploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy
Binolfi, A., Valiente‐Gabioud, A. A., Durán, R., Zweckstetter, M., Griesinger, C., & Fernández, C. O. (2010) · Journal of the American Chemical Society · doi:10.1021/ja107842f · Cited by 86 · see citing works
Faller, P., Hureau, C., Dorlet, P., Hellwig, P., Coppel, Y., Collin, F., & Aliès, B. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.015 · Cited by 86 · see citing works
Self-citationJiang, D., Li, X., Liu, L., Yagnik, G. B., & Zhou, F. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp9095375 · Cited by 83 · see citing works
Pedersen, J. T., Chen, S. W., Borg, C. B., Ness, S., Bahl, J. M. C., Heegaard, N. H. H., Dobson, C. M., Hemmingsen, L., Cremades, N., & Teilum, K. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b13577 · Cited by 81 · see citing works
Cheignon, C., Faller, P., Testemale, D., Hureau, C., & Collin, F. (2016) · Metallomics · doi:10.1039/c6mt00150e · Cited by 81 · see citing works
Self-citationYoung, T. R., Kirchner, A., Wedd, A. G., & Xiao, Z. (2014) · Metallomics · doi:10.1039/c4mt00001c · Cited by 72 · see citing works
Aliès, B., Sasaki, I., Proux, O., Sayen, S., Guillon, E., Faller, P., & Hureau, C. (2013) · Chemical Communications · doi:10.1039/c2cc38236a · Cited by 68 · see citing works
Self-citationCamponeschi, F., Valensin, D., Tessari, I., Bubacco, L., Dell’Acqua, S., Casella, L., Monzani, E., Gaggelli, E., & Valensin, G. (2013) · Inorganic Chemistry · doi:10.1021/ic302050m · Cited by 65 · see citing works
Yako, N., Young, T. R., Cottam, J. M., Hutton, C. A., Wedd, A. G., & Xiao, Z. (2017) · Metallomics · doi:10.1039/c6mt00299d · Cited by 46 · see citing works
Copper(I/II), α/β‐Synuclein and Amyloid‐β: Menage à Trois?
Ricco, R. D., Valensin, D., Dell’Acqua, S., Casella, L., Hureau, C., & Faller, P. (2015) · ChemBioChem · doi:10.1002/cbic.201500425 · Cited by 44 · see citing works
Self-citationAliès, B., Bijani, C., Sayen, S., Guillon, E., Faller, P., & Hureau, C. (2012) · Inorganic Chemistry · doi:10.1021/ic302097d · Cited by 44 · see citing works
Self-citationAtrián‐Blasco, E., Cerrada, E., Conte‐Daban, A., Testemale, D., Faller, P., Laguna, M., & Hureau, C. (2015) · Metallomics · doi:10.1039/c5mt00077g · Cited by 42 · see citing works
Self-citationCheignon, C., Collin, F., Faller, P., & Hureau, C. (2016) · Dalton Transactions · doi:10.1039/c6dt01979j · Cited by 39 · see citing works
Self-citationTrujano-Ortiz, L. G., González, F. J., & Quintanar, L. (2014) · Inorganic Chemistry · doi:10.1021/ic501941a · Cited by 38 · see citing works
Noël, S., Perez, F., Pedersen, J. T., Aliès, B., Mallet‐Ladeira, S., Sayen, S., Guillon, E., Gras, E., & Hureau, C. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.05.016 · Cited by 37 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Atrián‐Blasco, E., Gonzalez, P., Santoro, A., Aliès, B., Faller, P., & Hureau, C. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.007 · Cited by 168 · see citing works
Self-citationGomes, L. M., Mahammed, A., Prosser, K. E., Smith, J. R., Silverman, M. A., Walsby, C. J., Gross, Z., & Storr, T. (2018) · Chemical Science · doi:10.1039/c8sc04660c · Cited by 56 · see citing works
CuII Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function
Stefaniak, E., & Bal, W. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01399 · Cited by 53 · see citing works
Binding and Reactivity of Copper to R1 and R3 Fragments of tau Protein
Bacchella, C., Gentili, S., Bellotti, D., Quartieri, E., Draghi, S., Baratto, M. C., Remelli, M., Valensin, D., Monzani, E., Nicolis, S., et al. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b02266 · Cited by 51 · see citing works
Current understanding of metal-dependent amyloid-β aggregation and toxicity
Yi, Y., & Lim, M. H. (2022) · RSC Chemical Biology · doi:10.1039/d2cb00208f · Cited by 50 · see citing works
Copper and cuproptosis: new therapeutic approaches for Alzheimer’s disease
Li, X., Chen, X., & Gao, X. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1300405 · Cited by 45 · see citing works
Impact of N‐Truncated Aβ Peptides on Cu‐ and Cu(Aβ)‐Generated ROS: Cu<sup>I</sup> Matters!
Esmieu, C., Ferrand, G., Borghesani, V., & Hureau, C. (2021) · Chemistry – A European Journal · doi:10.1002/chem.202003949 · Cited by 43 · see citing works
Self-citationArrigoni, F., Prosdocimi, T., Mollica, L., GIOIA, L. D., Zampella, G., & Bertini, L. (2018) · Metallomics · doi:10.1039/c8mt00216a · Cited by 42 · see citing works
Han, J., Lee, H. J., Kim, K. Y., Nam, G., Chae, J., & Lim, M. H. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1916944117 · Cited by 37 · see citing works
Redox processes in Cu-binding proteins: the “in-between” states in intrinsically disordered peptides
Falcone, E., & Hureau, C. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00443k · Cited by 17 · see citing works
Self-citationStructural analysis of copper(I) interaction with amyloid β peptide
Gregorio, G. D., Biasotto, F., Hecel, A., Łuczkowski, M., Kozłowski, H., & Valensin, D. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.03.006 · Cited by 34 · see citing works
Streltsov, V. A., Ekanayake, R. S. K., Drew, S. C., Chantler, C. T., & Best, S. P. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b01255 · Cited by 34 · see citing works
Csire, G., Canabady‐Rochelle, L., Averlant‐Petit, M., Selmeczi, K., & Stefan, L. (2020) · Metallomics · doi:10.1039/d0mt00103a · Cited by 31 · see citing works
Ma, X., Wang, Y., Hua, J., Xu, C., Yang, T., Yuan, J., Chen, G., Guo, Z., & Wang, X. (2019) · Science China Chemistry · doi:10.1007/s11426-019-9594-y · Cited by 30 · see citing works
Bacchella, C., Dell'Acqua, S., Nicolis, S., Monzani, E., & Casella, L. (2022) · Coordination chemistry reviews · doi:10.1016/j.ccr.2022.214756 · Cited by 25 · see citing works
Aβ5– x Peptides: N-Terminal Truncation Yields Tunable Cu(II) Complexes
Wezynfeld, N. E., Tobolska, A., Mital, M., Wawrzyniak, U. E., Wiloch, M. Z., Płonka, D., Bossak‐Ahmad, K., Wróblewski, W., & Bal, W. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c01773 · Cited by 26 · see citing works
Okafor, M., Gonzalez, P., Ronot, P., Masoudi, I. E., Boos, A., Ory, S., Chasserot‐Golaz, S., Gasman, S., Raibaut, L., Hureau, C., et al. (2022) · Chemical Science · doi:10.1039/d2sc02593k · Cited by 26 · see citing works
Self-citationDey, C., Roy, M., Pal, P., Ghosh, R., & Dey, S. G. (2025) · Chemical Society Reviews · doi:10.1039/d5cs00544b · Cited by 21 · see citing works
Copper Transporters? Glutathione Reactivity of Products of Cu–Aβ Digestion by Neprilysin
Stefaniak, E., Płonka, D., Szczerba, P., Wezynfeld, N. E., & Bal, W. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c00427 · Cited by 20 · see citing works
Przygońska, K., Pacewicz, M., Sadowska, W., Poznański, J. T., Bal, W., & Dadlez, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-45988-1 · Cited by 18 · see citing works
Falco, A. D., Kincheski, G. C., Atrián‐Blasco, E., Hureau, C., Ferreira, S. T., & Rey, N. A. (2020) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000578 · Cited by 17 · see citing works
Self-citationBio-Inspired Casein-Derived Antioxidant Peptides Exhibiting a Dual Direct/Indirect Mode of Action
Csire, G., Dupire, F., Canabady‐Rochelle, L., Selmeczi, K., & Stefan, L. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c03085 · Cited by 16 · see citing works
Oxidative Damages on the Alzheimer’s Related-Aβ Peptide Alters Its Ability to Assemble
Cheignon, C., Collin, F., Sabater, L., & Hureau, C. (2023) · Antioxidants · doi:10.3390/antiox12020472 · Cited by 16 · see citing works
Self-citationKola, A., Vigni, G., Baratto, M. C., & Valensin, D. (2023) · Molecules · doi:10.3390/molecules28186629 · Cited by 16 · see citing works
Kola, A., Lamponi, S., Currò, F., & Valensin, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032500 · Cited by 16 · see citing works
Carvalho, A., Barbosa, B. M., Flores, J. S., Gonçalves, P. D. C., Diniz, R., Cordeiro, Y., Fernández, C. O., Cukierman, D. S., & Rey, N. A. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.112033 · Cited by 15 · see citing works
Unexpected Trends in Copper Removal from Aβ Peptide: When Less Ligand Is Better and Zn Helps
Esmieu, C., Balderrama-Martínez-Sotomayor, R., Conte‐Daban, A., Iranzo, O., & Hureau, C. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c03407 · Cited by 14 · see citing works
Self-citationMicera, A., Bruno, L., Cacciamani, A., Rongioletti, M. C. A., & Squitti, R. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191023114015 · Cited by 13 · see citing works
Atrián‐Blasco, E., Cerrada, E., Faller, P., Laguna, M., & Hureau, C. (2019) · Metallomics · doi:10.1039/c9mt00011a · Cited by 12 · see citing works
Self-citationBacchella, C., Dell’Acqua, S., Nicolis, S., Monzani, E., & Casella, L. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c02243 · Cited by 12 · see citing works
Rulmont, C., Stigliani, J., Hureau, C., & Esmieu, C. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.3c02693 · Cited by 11 · see citing works
Self-citationCombating multiple aetiologies of Alzheimer's disease to rescue behavioural deficits
Ramesh, M., Balachandra, C., Kumar, A., Samanta, S., & Govindaraju, T. (2025) · Chemical Science · doi:10.1039/d4sc08585j · Cited by 10 · see citing works
Arrigoni, F., Rizza, F., Tisi, R., GIOIA, L. D., Zampella, G., & Bertini, L. (2020) · Metallomics · doi:10.1039/d0mt00113a · Cited by 10 · see citing works
Drommi, M., Rulmont, C., Esmieu, C., & Hureau, C. (2021) · Molecules · doi:10.3390/molecules26247630 · Cited by 10 · see citing works
Self-citationLakela, A. L., Berntsson, E., Vosough, F., Jarvet, J., Paul, S., Barth, A., Gräslund, A., Roos, P. M., & Wärmländer, S. K. T. S. (2025) · Scientific Reports · doi:10.1038/s41598-024-59826-6 · Cited by 9 · see citing works
Aliès, B., Borghesani, V., Noël, S., Sayen, S., Guillon, E., Testemale, D., Faller, P., & Hureau, C. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201802759 · Cited by 10 · see citing works
Self-citationTobolska, A., Głowacz, K., Ciosek, P., Bal, W., Wróblewski, W., & Wezynfeld, N. E. (2022) · Dalton Transactions · doi:10.1039/d2dt03078k · Cited by 9 · see citing works
Malikidogo, K. P., Drommi, M., Atrián‐Blasco, E., Hormann, J., Kulak, N., Esmieu, C., & Hureau, C. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202203667 · Cited by 9 · see citing works
Self-citationMagrì, A. L., Tomasello, B., Николаевна, Н. И., Tabbı̀, G., Cairns, W. R. L., Greco, V., Sciuto, S., Mendola, D. L., & Rizzarelli, E. (2024) · Biomolecules · doi:10.3390/biom14091104 · Cited by 9 · see citing works
Bacchella, C., Caro, S. D., Nicolis, S., Monzani, E., & Dell’Acqua, S. (2024) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2024.112775 · Cited by 6 · see citing works
Superoxide Reduction by Cu‐Amyloid Beta Peptide Complexes: A Density Functional Theory Study
Arrigoni, F., Carlo, C. D., Rovetta, A., GIOIA, L. D., Zampella, G., & Bertini, L. (2022) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202200245 · Cited by 7 · see citing works
Wezynfeld, N. E., Vileno, B., & Faller, P. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b00711 · Cited by 6 · see citing works
Self-citationMital, M., Szutkowski, K., Bossak‐Ahmad, K., Skrobecki, P., Drew, S., Poznański, J., Zhukov, I., Frączyk, T., & Bal, W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239200 · Cited by 3 · see citing works
Sudzik, D., Bal, W., & Wezynfeld, N. E. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70145 · Cited by 4 · see citing works
Berthonnaud, L., Esmieu, C., Mallet‐Ladeira, S., & Hureau, C. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111601 · Cited by 4 · see citing works
Self-citationTomasello, M. F., Di Rosa, M. C., Naletova, I., Sciacca, M. F. M., Giuffrida, A., Maccarrone, G., & Attanasio, F. (2025) · Bioinorganic Chemistry and Applications · doi:10.1155/bca/4226220 · Cited by 3 · see citing works
“Tis behavior is in agreement with literature data which report a moderate ROS generation of a β :Cu(II) complex compared to “free” copper, due to a more difcult redox-cycling [35, 79].”
Molecular dynamics simulations of copper binding to N-terminus mutants of amyloid-β
Kennedy-Britten, O. D., Alshammari, N., & Platts, J. A. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1745692 · Cited by 3 · see citing works
Investigating Cu(I) binding to model peptides of N-terminal Aβ isoforms
Hjelmstad, A. S., Pushie, M. J., Ruth, K., Escobedo, M., Kuter, K. E., & Haas, K. L. (2024) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2024.112480 · Cited by 3 · see citing works
The Angiotensin Metabolite His-Leu Is a Strong Copper Chelator Forming Highly Redox Active Species
Wezynfeld, N., Sudzik, D., Tobolska, A., Makarova, K., Stefaniak, E., Frączyk, T., Wawrzyniak, U. E., & Bal, W. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c01640 · Cited by 3 · see citing works
Accelerated Molecular Dynamics to Explore the Binding of Transition Metals to Amyloid-β
Kennedy-Britten, O. D., Alshammari, N., & Platts, J. A. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00466 · Cited by 3 · see citing works
Fusobacterium nucleatum’s Copper-FomA Proteins: Driving Cancer Forward
Lesiów, M. K., Kwiatkowski, B., Pietrzyk, P., Kyzioł, A., Rolka, K., & Komarnicka, U. K. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5c01747 · Cited by 2 · see citing works
Walencik, P. K. (2022) · Dalton Transactions · doi:10.1039/d2dt02398a · Cited by 2 · see citing works
Exploration of Lycorine and Copper(II)’s Association with the N-Terminal Domain of Amyloid β
Kola, A., Vigni, G., & Valensin, D. (2023) · Inorganics · doi:10.3390/inorganics11110443 · Cited by 2 · see citing works
Suseela, Y. V., Mandal, S. K., Jacquemin, D., Govindaraju, T., & Faller, P. (2025) · Chemistry - A European Journal · doi:10.1002/chem.202502598 · Cited by 1 · see citing works
Self-citationDrommi, M., Malikidogo, K. P., Atrián‐Blasco, E., Esmieu, C., & Hureau, C. (2025) · Chemistry - A European Journal · doi:10.1002/chem.202502352
Self-citationSynthesis and characterization of copper-peptide systems for oxidation catalysis
Hautier, A. (2018) · theses.fr (ABES) · doi:10.70675/42dc4706z4ad1z44e2z856bz4728905aa267
Peptides as unique tools to modulate redox levels: towards applications in living cells and in vivo
Balbali, N., & Delsuc, N. (2026) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2026.100079
Cerlati, O., Putaux, J., Marty, J., Mingotaud, A., Vicendo, P., Pimienta, V., & Collin, F. (2026) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2026.141831
Malpani, P., Bhatt, S., Mehta, A., Bhuvanesh, N. S. P., Joshi, H., & Sharma, A. K. (2026) · Inorganica Chimica Acta · doi:10.1016/j.ica.2026.123496
- Authors
- Atrián-Blasco, E., del Barrio, M., Faller, P., & Hureau, C.
- Affiliations
- LCC-CNRS, Université de Toulouse, CNRS, Toulouse, France
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Faller, Peter
- Hureau, Christelle
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-04-03
- Volume
- 90
- Issue
- 9
- Pages
- 5909-5915
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- PMC
- PMC6120677
- OpenAlex
- W2795843933
- Cited by
- 62
- References
- 50
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 6 · 2023: 7 · 2022: 10 · 2021: 5 · 2020: 9 · 2019: 8 · 2018: 6
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Agence Nationale de la Recherche (ANR-13-BSV5-0016)
- H2020 European Research Council (638712)
- Universit? de Strasbourg Institut d'?tudes Avanc?es
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- amyloid-beta, copper complexes, ascorbic acid oxidation, reactive oxygen species, oxidative stress, Alzheimer's disease, key residues
- MeSH terms
- Amino Acid Sequence, Copper, Organometallic Compounds, Oxidation-Reduction, Amyloid beta-Peptides, Reactive Oxygen Species
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review