Interaction of Cobalt Tetrasulfophthalocyanine with ORF8 Accessory Protein of SARS-CoV-2

O. I. Koifman; Койфман О. И.; V. E. Maizlish; Майзлиш В. Е.; N. Sh. Lebedeva; Лебедева Н. Ш.; E. S. Yurina; Юрина Е. С.; S. S. Guseinov; Гусейнов С. С.; E. L. Guriev; Гурьев Е. Л.; Yu. A. Gubarev; Губарев Ю. А.

doi:10.31857/S0132344X23600042

Interaction of Cobalt Tetrasulfophthalocyanine with ORF8 Accessory Protein of SARS-CoV-2

作者: Koifman O.I.¹^,2, Maizlish V.E.², Lebedeva N.S.¹, Yurina E.S.¹, Guseinov S.S.¹, Guriev E.L.³, Gubarev Y.A.¹
隶属关系:
1. G.A. Krestov Institute of Solution Chemistry of the Russian Academy of Sciences, Ivanovo, Russia
2. Ivanovo State University of Chemical Technology, Ivanovo, Russia
3. Lobachevsky State University of Nizhny Novgorod, Nizhny Novgorod, Russia
期: 卷 49, 编号 10 (2023)
页面: 659-664
栏目: Articles
URL: https://journals.eco-vector.com/0132-344X/article/view/667477
DOI: https://doi.org/10.31857/S0132344X23600042
EDN: https://elibrary.ru/TCRLOA
ID: 667477

如何引用文章

全文:

开放存取

##reader.subscriptionAccessGranted##
受限制的访问

订阅存取

详细
作者简介
参考
补充文件
统计

详细

The interaction of cobalt(II) tetrasulfophthalocyanine (CoPc) with the ORF8 accessory protein of SARS-CoV-2 was studied by spectroscopy and calorimetry. The protein was found to shift the aggregation equilibrium in cobalt tetrasulfophthalocyanine solutions towards dimerization. Most probably, the CoPc dimer binds to ORF8 on the greater β-sheet side, thus causing fluorescence quenching. The protein affinity constant to CoPc dimer is 1.5 × 105. Differential scanning calorimetry data indicate that ORF8 undergoes thermally induced denaturation in the temperature range of 38–67°C. Melting of ORF8 includes two stages, which partly overlap. The complex formation of ORF8 with CoPc leads to thermal stabilization of the protein, thus preventing the second stage of protein unfolding. Denaturation of the complex proceeds between 40 and 77°C as two temperature-separated stages. According to gel electrophoresis and immunoblotting data, visible light photoirradiation of the ORF8 complex with CoPc does not induce photooxidation of the protein. It was shown that water-soluble cobalt sulfo-substituted phthalocyanine can be considered as a potential drug inhibiting the ORF8 accessory protein.

关键词

SARS-CoV-2, metal phthalocyanines, protein, complex, photoinactivation

参考

Garcia-Vidal C., Meira F., Cózar-Llistó A. et al. // Revista Española de Quimioterapia. 2021. V. 34. P. 136. https://doi.org/10.37201/req/018.2021
Benfield T., Bodilsen J., Brieghel C. et al. // Clin. Infect. Dis. 2021. V. 73. P. 2031. https://doi.org/10.1093/cid/ciab536
Koifman O., Ageeva T., Kuzmina N.S. // Macroheterocycles. 2022. V. 15. P. 207. https://doi.org/10.6060/mhc224870k
Lebedeva N.S., Gubarev Y.A., Koifman M.O. et al. // Molecules. 2020. V. 25. P. 4368. https://doi.org/10.3390/molecules25194368
Gubarev Y.A., Lebedeva N.S., Yurina E.S. et al. // J. Biomol. Struct. Dyn. 2022. P. 1. https://doi.org/10.1080/07391102.2022.2079562
Lebedeva N.S., Gubarev Y.A., Mamardashvili G.M. et al. // Sci. Reports. 2021. V. 11. P. 1. https://doi.org/10.1038/s41598-021-99072-8
Koifman O.I., Lebedeva N.S., Gubarev Y.A. et al. // Chem. Heterocycl. Compd. 2021. V. 57. P. 423. https://doi.org/10.1007/s10593-021-02920-8
Koifman M.O., Malyasova A.S., Romanenko Y.V. et al. // Spectrochim. Acta. A. 2022. V. 279. P. 121403. https://doi.org/https://doi.org/10.1016/j.saa.2022.121403
Koifman O.I., Ageeva T.A., Beletskaya I.P. et al. // Macroheterocycles. 2020. V. 13. https://doi.org/10.6060/mhc200814k
Weber J.H., Busch D.H. // Inorg. Chem. 1965. V. 4. P. 469. https://doi.org/10.1021/ic50026a007
Шапошников Г., Кулинич В., Майзлиш В. Модифицированные фталоцианины и их структурные аналоги. М.: Красанд, 2012.
Майзлиш В., Мочалова Н., Снегирева Ф. и др. // Изв. вузов. Хим. и хим. технол. 1986. Т. 29. P. 3.
Trott O., Olson A.J. // J. Comput. Chem. 2010. V. 31. P. 455. https://doi.org/10.1002/jcc.21334
Zhang C., Zheng W., Huang X. et al. // J. Proteome Res. 2020. V. 19. P. 1351. https://doi.org/10.1021/acs.jproteome.0c00129
Zheng W., Zhang C., Li Y. et al. // Cell Reports Methods. 2021. P. 100014. https://doi.org/10.1016/j.crmeth.2021.100014
Neese F. // Wiley Interdiscip. Rev. Comput. Mol. Sci. 2022. V. 12. Art. e1606. https://doi.org/10.1002/wcms.1606
Baker N.A., Sept D., Joseph S. et al. // Proc. Natl. Acad. Sci. U.S.A. 2001. V. 98. P. 10037. https://doi.org/10.1073/pnas.181342398
Zhang Y., Chen Y., Li Y. et al. // Proc. Natl. Acad. Sci. U.S.A. 2021. V. 118. Art. e2024202118. https://doi.org/10.1073/pnas.2024202118
Li J.-Y., Liao C.-H., Wang Q. et al. // Virus Res. 2020. V. 286. P. 198074. https://doi.org/10.1016/j.virusres.2020.198074
Lebedeva N.S., Yurina E.S., Gubarev Y.A. et al. // J. Photochem. Photobiol. A. 2018. V. 353. P. 299. https://doi.org/10.1016/j.jphotochem.2017.11.037
Lebedeva N.S., Popova T., Mal’kova E. et al. // Russ. J. Phys. Chem. A. 2013. V. 87. P. 2030. https://doi.org/10.1134/S0036024413120133
Flower T.G., Buffalo C.Z., Hooy R.M. et al. // Proc. Natl. Acad. Sci. U.S.A. 2021. V. 118. Art. e2021785118. https://doi.org/10.1073/pnas.2021785118