RAS Chemistry & Material ScienceХимическая физика Advances in Chemical Physics

  • ISSN (Print) 0207-401X
  • ISSN (Online) 3034-6126

Antioxidant activity of catecholamines during the oxidation of methyl linoleoate in Triton X-100 micelles

PII
10.31857/S0207401X24090042-1
DOI
10.31857/S0207401X24090042
Publication type
Article
Status
Published
Authors
Volume/ Edition
Volume 43 / Issue number 9
Pages
35-41
Abstract
The effect of catecholamines on the oxidation of methyl linoleate in Triton X-100 micelles was studied. It has been established that catecholamines do not inhibit oxidation at a pH 7.4. Inhibition is only possible in the presence of the superoxide dismutase enzyme or at lower pH levels. The reason for this effect is the interaction of anionic forms of phenols and phenoxyl radicals with oxygen with the formation of superoxide anions. High values of inhibition coefficients for catecholamines in the presence of superoxide dismutase are due to the reactions of the resulting ortho-quinones, leading to the regeneration of OH groups.
Keywords
катехоламины метиллинолеат антиоксидантная активность супероксидный анион-радикал супероксиддисмутаза
Date of publication
12.09.2024
Year of publication
2024
Number of purchasers
0
Views
47

References

  1. 1. Tikhonov I., Roginsky V., Pliss E. // Intern. J. Chem. Kinet. 2008. V. 41. № 2. P. 92; https://doi.org/10.1002/kin.20377
  2. 2. Tichonov I., Roginsky V., Pliss E. // Eur. J. Lipid Sci. Technol. 2010. V. 112. № 8. P. 887; https://doi.org/10.1002/ejlt.200900282
  3. 3. Roginsky V. // Arch. Biochem. Biophys. 2003. V. 414. № 2. P. 261; https://doi.org/10.1016/S0003-9861 (03)00143-7
  4. 4. Roginsky V., Lissi E.A. // Food Chem. 2005. V. 92. № 2. P. 235; https://doi.org/10.1016/j.foodchem.2004.08.004
  5. 5. Jodko-Piorecka K., Litwinienko G. // Free Radic. Biol. Med. 2015. V. 83. P. 1; https://doi.org/10.1016/j.freeradbiomed.2015.02.006
  6. 6. Loshadkin D., Roginsky V., Pliss E. // Intern. J. Chem. Kinet. 2002. V. 34. № 3. P. 162; https://doi.org/10.1002/kin.10041
  7. 7. Roginsky V., Barsukova T. // Chem. Phys. Lipids. 2001. V. 111. № 1. P. 87; https://doi.org/10.1016/S0009-3084 (01)00148-7
  8. 8. Roginsky V., Barsukova T., Loshadkin D., Pliss E. // Chem. Phys. Lipids. 2003. V. 125. № 1. P. 49; https://doi.org/10.1016/S0009-3084 (03)00068-9
  9. 9. Roginsky V. // Free Radic. Res. 2001. V. 35. № 1. P. 55; https://doi.org/10.1080/10715760100300591
  10. 10. Москаленко И.В., Тихонов И.В. // Хим. физика. 2022. Т. 41. № 7. С. 18.
  11. 11. Costa V.M., Silva R., Ferreira L.M. et al. // Chem. Res. Toxicol. 2007. V. 20. № 8. P. 1183; https://doi.org/10.1021/tx7000916
  12. 12. Sirota T.V. // Biophysics. 2020. V. 65. P. 548; https://doi.org/10.1134/S0006350920040223
  13. 13. Mautjana N.A., Estes J., Eyler J.R. , Brajter-Toth A. // Electroanalysis. 2008. V. 20. № 18. P. 1959; https://doi.org/10.1002/elan.200804279
  14. 14. Iftikhar I., Abou El-Nour K., Brajter-Toth A. // Electrochim. Acta. 2017. V. 249. P. 145. https://doi.org/10.1016/j.electacta.2017.07.087
  15. 15. Русина И.Ф., Вепринцев Т.Л., Васильев Р.Ф. // Хим. физика. 2022. Т. 41. № 2. С. 12.
  16. 16. Mack F., Bonisch H. // Naunyn-Schmiedeberg‘s Arch. Pharmacol. 1979. V. 310. P. 1; https://doi.org/10.1007/BF00499868
  17. 17. Герасимов Н.Ю., Неврова О.В., Жигачева И.В., Генерозова И.П., Голощапов А.Н. // Хим. физика. 2023. Т. 42. № 1. С. 22.
  18. 18. Шишкина Л.Н., Козлов М.В., Константинова Т.В., Смирнова А.В., Швыдкий В.О. // Хим. физика. 2023. Т. 42. № 1. С. 28.
  19. 19. Jodko-Piorecka K., Sikora B., Kluzek M., Przybylski P., Litwinienko G. // J. Org. Chem. 2022. V. 87. № 3. P. 1791; https://doi.org/10.1021/acs.joc.1c02308
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