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Affinity and Effect of Anticancer Drugs on the Redox Reactivity of Hemoglobin

  • Cristina Puscas
    Cristina Puscas
    Department of Chemistry, Babes-Bolyai University, 1 Mihail Kogalniceanu Street, Cluj-Napoca 400084, Romania
  • Alina Mircea
    Alina Mircea
    Department of Chemistry, Babes-Bolyai University, 1 Mihail Kogalniceanu Street, Cluj-Napoca 400084, Romania
    More by Alina Mircea
  • Madalina Raiu
    Madalina Raiu
    Department of Chemistry, Babes-Bolyai University, 1 Mihail Kogalniceanu Street, Cluj-Napoca 400084, Romania
  • Mihaela Mic
    Mihaela Mic
    Department of Molecular and Biomolecular Physics, National Institute of Isotopic and Molecular Technologies, 400293 Cluj-Napoca, Romania
    More by Mihaela Mic
  • Amr A. A. Attia
    Amr A. A. Attia
    Department of Chemistry, Babes-Bolyai University, 1 Mihail Kogalniceanu Street, Cluj-Napoca 400084, Romania
  • , and 
  • Radu Silaghi-Dumitrescu*
    Radu Silaghi-Dumitrescu
    Department of Chemistry, Babes-Bolyai University, 1 Mihail Kogalniceanu Street, Cluj-Napoca 400084, Romania
    *E-mail: [email protected]
Cite this: Chem. Res. Toxicol. 2019, 32, 7, 1402–1411
Publication Date (Web):June 21, 2019
https://doi.org/10.1021/acs.chemrestox.9b00094
Copyright © 2019 American Chemical Society

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    Abstract

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    Hemoglobin’s redox reactivity is affected by anticancer drugs of the antitubulin class. Direct binding of these drugs to hemoglobin, with biomedically relevant affinities, is demonstrated. While this interaction is mostly allosteric, in the case of docetaxel, a direct redox reaction is also observed—correlating well with structural differences between the four compounds. A role for Tyr145 in this reactivity is proposed, in line with previous observations of the importance of this amino acid in the reactivity of Hb toward agents of oxidative stress. A susceptibility of vinorelbin (and to a lower extent of paclitaxel) toward peroxide and peroxidase is shown.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.chemrestox.9b00094.

    • Autooxidation rates of hemoglobin in the presence of irinotecan and vinorelbine and raw data for the nitrite-induced autoxidation of hemoglobin experiment (PDF)

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    Cited By

    This article is cited by 5 publications.

    1. Cezara Zagrean-Tuza, Ilinca Igescu, Alexandru Lupan, Radu Silaghi-Dumitrescu. A study of the molecular interactions of hemoglobin with diverse classes of therapeutic agents. Inorganica Chimica Acta 2024, 567 , 122053. https://doi.org/10.1016/j.ica.2024.122053
    2. Dana Elena Popa, Iulia Gabriela David, Mihaela Carmen Cheregi, Emilia Elena Iorgulescu, Mihaela Buleandră. (Bio)electroanalysis of microtubule-targeting agents used in cancer chemotherapy. Microchemical Journal 2023, 192 , 108965. https://doi.org/10.1016/j.microc.2023.108965
    3. Hassan A. Alhazmi, Md Shamsher Alam, Mohammed Albratty, Asim Najmi, Ahmed A. Abdulhaq, Rym Hassani, Waquar Ahsan, Abdulrahman N. Qramish, . Binding Investigation of Some Important Metal Ions Copper (I), Nickel (II), and Aluminium (III) with Bovine Serum Albumin Using Valid Spectroscopic Techniques. Journal of Chemistry 2023, 2023 , 1-10. https://doi.org/10.1155/2023/2581653
    4. Jing Tu, Min Tang, Guoqing Li, Liang Chen, Yong Huang, . Molecular Typing Based on Oxidative Stress Genes and Establishment of Prognostic Characteristics of 7 Genes in Lung Adenocarcinoma. Oxidative Medicine and Cellular Longevity 2022, 2022 , 1-34. https://doi.org/10.1155/2022/9683819
    5. Francisco Carrascoza, Radu Silaghi-Dumitrescu. The dynamics of hemoglobin-haptoglobin complexes. Relevance for oxidative stress. Journal of Molecular Structure 2022, 1250 , 131703. https://doi.org/10.1016/j.molstruc.2021.131703

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