Proteinase resistance of carnosine, pyrrolylcarnosine, and salicylcarnosine
- Authors: Shevchenko K.V.1, Nagaev I.Y.1, Kulikova O.I.2, Stvolinsky S.L.2, Shevchenko V.P.1, Myasoedov N.F.1
-
Affiliations:
- National Research Centre “Kurchatov Institute”
- Research Center of Neurology
- Issue: Vol 50, No 2 (2024)
- Pages: 146–152
- Section: Articles
- URL: https://journals.rcsi.science/0132-3423/article/view/258833
- DOI: https://doi.org/10.31857/S0132342324020042
- EDN: https://elibrary.ru/ONHXKY
- ID: 258833
Cite item
Open Access
Access granted
Abstract
The stability of carnosine, pyrrolylcarnosine (PC) and salicylcarnosine (SC) to the action of leucine aminopeptidase, carboxypeptidases B and Y was evaluated. It was found that proteolysis of carnosine, PC and SC under the action of leucine aminopeptidase does not occur. Carboxypeptidases B and Y, as well as the enzyme system of blood plasma and plasma membranes of rat brain cells, degraded peptides containing β-alanyl, N-pyrrolyl, N-salicylic fragments to varying degrees. In all cases, histidine is formed. The formation of pyrrole or salicylic acid does not occur. It was found that carnosine, PC and SC showed high stability to the action of amino- and carboxypeptidases in in vitro experiments.
Keywords
Full Text
About the authors
K. V. Shevchenko
National Research Centre “Kurchatov Institute”
Author for correspondence.
Email: ATCarma@mail.ru
Russian Federation, 123182, Moscow, pl. Kurchatova 2
I. Yu. Nagaev
National Research Centre “Kurchatov Institute”
Email: ATCarma@mail.ru
Russian Federation, 123182, Moscow, pl. Kurchatova 2
O. I. Kulikova
Research Center of Neurology
Email: ATCarma@mail.ru
Russian Federation, 125367, Moscow, Volokolamskoe shosse 80
S. L. Stvolinsky
Research Center of Neurology
Email: ATCarma@mail.ru
Russian Federation, 125367, Moscow, Volokolamskoe shosse 80
V. P. Shevchenko
National Research Centre “Kurchatov Institute”
Email: ATCarma@mail.ru
Russian Federation, 123182, Moscow, pl. Kurchatova 2
N. F. Myasoedov
National Research Centre “Kurchatov Institute”
Email: ATCarma@mail.ru
Russian Federation, 123182, Moscow, pl. Kurchatova 2
References
- Agyei D., Ahmed I., Akram Z., Iqbal H.M.N., Danquah M.K. // Protein Pept. Lett. 2017. V. 24. P. 94–101. https://doi.org/10.2174/0929866523666161222150444
- Boldyrev A.A., Aldini G., Derave W. // Physiol. Rev. 2013. V. 93. P. 1803–1845. https://doi.org/10.1152/physrev.00039.2012
- Hipkiss A.R. // In: Advances in Food and Nutrition Research / Ed. Taylor S.L. Burlington: Academic Press, 2009. V. 57. P. 87–154.
- Bellia F., Vecchio G., Rizzarelli E. // Molecules. 2014. V. 19. P. 2299–2329. https://doi.org/10.3390/molecules19022299
- Танашян М.М., Федорова Т.Н., Стволинский С.Л., Андреева Л.А., Нагаев И.Ю., Мигулин В.А., Шаба- лина А.А., Трубицына И.Е., Лопачев А.В., Куликова О.И., Абаимов Д.А. // Патент RU 2694061 C1, опубл. 09.07.2019.
- Федорова Т.Н., Стволинский С.Л., Мигулин В.А., Лопачев А.В., Хуторова А.В., Куликова О.И., Музы- чук О.А., Абаимов Д.А. // Патент RU 2777391 С1, опубл. 03.08.2022.
- Baltazar M.T., Dinis-Oliveira R.J., Duarte J.A., Bastos M.L., Carvalho F. // Curr. Med. Chem. 2011. V. 18. P. 3252–3264. https://doi.org/10.2174/092986711796391552
- Bhardwaj V., Gumber D., Abbot V., Dhimana S., Shar- ma P. // RSC Adv. 2015. V. 5. P. 15233–15266. https://doi.org/10.1039/C4RA15710A
- Pegova A., Abe H., Boldyrev A. // Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2000. V. 127. P. 443–446. https://doi.org/10.1016/S0305-0491(00)00279-0
- Шевченко К.В., Нагаев И.Ю., Андреева Л.А., Шевченко В.П., Мясоедов Н.Ф. // Биомед. химия. 2019. Т. 65. № 3. С. 180–201. [Shevchenko K.V., Nagaev I.Yu., Andreeva L.A., Shevchenko V.P., Myasoedov N.F. // Biochem. Moscow Suppl. Ser. B Biomed. Chem. 2019. V. 13. P. 179–201.] https://doi.org/10.1134/S1990750819030089
- Овчинников Ю.А. // Биоорганическая химия. М.: Просвещение, 1987.
Supplementary files
