Synthesis, Structure, and Properties of the Iron Nitrosyl Complex with 2-Ethyl-4-pyridinecarbothioamide

N. A. Sanina; Санина Н. А.; G. V. Shilov; Шилов Г. В.; N. S. Ovanesyan; Ованесян Н. С.; V. A. Mumyatova; Мумятова В. А.; A. A. Balakina; Балакина А. А.; A. A. Terent’ev; Терентьев А. А.; O. V. Pokidova; Покидова О. В.; S. M. Aldoshin; Алдошин С. М.

doi:10.31857/S0132344X23600169

Synthesis, Structure, and Properties of the Iron Nitrosyl Complex with 2-Ethyl-4-pyridinecarbothioamide

Authors: Sanina N.A.¹^,2^,3, Shilov G.V.¹, Ovanesyan N.S.¹, Mumyatova V.A.¹, Balakina A.A.¹, Terent’ev A.A.¹^,2^,3, Pokidova O.V.¹, Aldoshin S.M.¹
Affiliations:
1. Federal Research Center of Problems of Chemical Physics and Medicinal Chemistry, Russian Academy of Sciences, Chernogolovka, Russia
2. Research and Education Center “Medicinal Chemistry” in Chernogolovka, State University of Education, Mytishchi, Moscow oblast, Russia
3. Moscow State University, Moscow, Russia
Issue: Vol 49, No 9 (2023)
Pages: 530-542
Section: Articles
URL: https://rjeid.com/0132-344X/article/view/667480
DOI: https://doi.org/10.31857/S0132344X23600169
EDN: https://elibrary.ru/WBRISE
ID: 667480

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Abstract
About the authors
References
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Abstract

The synthesis and data on the physicochemical characteristics and biological activity of the new
iron nitrosyl complex (Q+)2[Fe2(S2O3)2(NO)4]2– (I), where Q+ is protonated 2-ethyl-4-pyridinecarbothioamide
(C8H11N2S), are presented. The structure and properties of the complex were studied by X-ray diffraction,
elemental analysis, IR and Mössbauer spectroscopy, and amperometry. The complex showed antibacterial
activity and efficiently inhibited cyclic guanosine monophosphate phosphodiesterase (cGMP PDE),
which may suggest its antihypertensive, anti-aggregation, and vasodilator activities.

Keywords

binuclear iron(I) tetranitrosyl complexes, X-ray diffraction, IR spectroscopy, Mössbauer spectroscopy, amperometry, antibacterial activity, biofilms, ampicillin, kanamycin, streptomycin, ceftriaxone, MTT assay, phosphodiesterase

About the authors

N. A. Sanina

Federal Research Center of Problems of Chemical Physics and Medicinal Chemistry, Russian Academy of Sciences,
Chernogolovka, Russia; Research and Education Center “Medicinal Chemistry” in Chernogolovka, State University of Education,
Mytishchi, Moscow oblast, Russia; Moscow State University, Moscow, Russia

Email: sanina@icp.ac.ru
Россия, Черноголовка; Россия, Мытищи; Россия, Москва

References

Benencia F., Courreges M.C. // Immunology.1999. V. 98. № 3. P. 363.
Mehta D.R., Ashkar A.A., Mossman K.L. // PLoS One. 2012. V. 7. № 2. Art. e31688.
McMullin B.B., Chittock D.R., Roscoe D.L. et al. // Respiratory Care. 2005. V. 50. № 11. P. 1451.
Jones-Carson J., Zweifel A.E., Tapscott T. et al. // PLoS Negl. Trop. Dis. 2014. V. 8. № 8. Art. e3079.
Fang F.C. // J. Clin. Invest. 1997. V. 99. № 12. P. 2818.
De Groote M.A., Fang F.C. // Clin. Infect. Dis. 1995. V. 21. № 2. P. S162.
Schairer D.O., Chouake J.S., Nosanchuk J.D. et al. // Virulence. 2012. V. 3. P. 271.
Jones M.L., Ganopolsky J.G., Labbe A. et al. // Appl. Microbiol. Biotechnol. 2010. V. 88. № 2. P. 401.
Jones M.L., Ganopolsky J.G., Labbe A. et al. // Appl. Microbiol. Biotechnol. 2010. V. 87. № 2. P. 509.
Fox S., Wilkinson T.S., Wheatley P.S. et al. // Acta Biomater. 2010. V. 6. № 4. P. 1515.
Narin G., Albayrak C.B., Ulku S. // Appl. Clay Sci. 2010. V. 50. № 4. P. 560.
Weller R., Ormerod A.D., Hobson R.P. et al. // J. Am. Acad. Dermatol. 1998. V. 38. № 4. P. 559.
Ormerod A.D., White M.I., Shah S.A. et al. // Br. J. Dermatol. 1999. V. 41. № 6. P. 1051.
Phillips R., Adjei O., Lucas S. et al. // Antimicrob. Agents Chemother. 2004. V. 48. № 8. P. 2866.
Ormerod A.D., Shah A.A., Li H. et al. // BMC Res. Notes. 2011. V. 4. P. 458.
Davidson R.N., Yardley V., Croft S.L. et al. // Trans. R. Soc. Trop. Med. Hyg. 2000. V. 94. № 3. P. 319.
Daiber A., Wenzel P., Oelze M. et al. // Clin. Res. Cardiol. 2008. V. 97. № 1. P. 12.
Deupree S.M., Schoenfisch M.H. // Acta Biomater. 2009. V. 5. № 5. P. 1405.
Schairer D.O., Chouake J.S., Nosanchuk J.D., Friedman A.J. // Virulence. 2012. V. 3. № 3. P. 271.
Cariello A.J., Bispo P.J., de Souza et al. // Clin. Ophthalmol. 2012. V. 6. P. 1907.
Williams D.L.H. // Acc. Chem. Res. 1999. V. 32. № 10. P. 869.
Laver J.R., Stevanin T.M., Messenger S.L. et al. // FASEB J. 2010. V. 24. № 1. P. 286.
Jaouen G., Salmain M. The Bioorganometalic Chemistry: Applications in Drug Discovery, Biocatalysis and Imaging. Weinheim: Wiley-VCH, 2014. 424 p.
Hsiao H., Chung C., Santos et al. // Dalton Trans. 2019. V. 48. P. 9431.
Gould N., Doulias P.-T., Tenopoulou M. et al. // J. Biol. Chem. 2013. V. 288. № 37. P. 26473.
Stupina T.S., Antonova N.O., Balalaeva et al. // Intern. Sci. J. Med. Biol. Sci. 2014. V. 1. № 1. P. 23.
Григорьев А.И., Владимиров Ю.А. Фундаментальные науки – медицине: Биофизические медицинские технологии. M.: МАКС Пресс, 2015. 448 с.
Санина Н.A., Козуб Г.И., Кондратьева T.A. и др. // Изв. АН. Сер. хим. 2017. № 9. С. 1706.
Мумятова В.А., Козуб Г.И., Кондратьева Т.А. и др. // Изв. АH. Сер. хим. 2019. № 5. С. 1025.
Санина Н.А., Мумятова В.А., Терентьев А.А. и др. // Изв. РАН. Сер. хим. 2019. № 12. С. 2225.
Hanoulle X., Wieruszeski J.M., Rouseelot-Pailley P. et al. // Biochem. Biophys. Res. Commun. 2005. V. 331. P. 452.
Vilchèze C., Weisbrod T.R., Chen B. et al. // Antimicrob. Agents Chemother. 2005. V. 49. P. 708.
Yu K.L., Torri A.F., Luo G. et al. // Bioorg. Med. Chem. Lett. 2002. V. 12. № 23. P. 3379.
Hitotsuyanagi Y., Hasuda T., Matsumoto Y. et al. // Chem. Commun. 2000. № 17. P. 1633.
Nakagawa Y., Irie K., Ohigashi H. et al. // Bioorg. Med. Chem. Lett. 2000. V. 10. № 18. P. 2087.
Wei Q.L., Zhang S.S., Gao J. et al. // Bioorg. Med. Chem. 2006. V. 14. № 21. P. 7146.
Wentland M.P., Sun X., Bu Y. et al. // Bioorg. Med. Chem. Lett. 2005. V. 15. № 10. P. 2547.
Krinková J., Doležal M., Hartl J. et al. // Il Farmaco. 2002. V. 57. № 1. P. 71.
Yu K.L., Torri A.F., Luo G. et al. // Bioorg. Med. Chem. Lett. 2002. V. 12. № 23. P. 3379.
Davies D.J., Faust R., Garratt P.J. et al. // Bioorg Chem. 2004. V. 32. № 1. P. 1.
Boström J., Olsson R.I., Tholander J. et al. // Bioorg. Med. Chem. Lett. 2010. V. 20. № 2. P. 479.
Thanigaimalai P., Sharma V.K., Lee K.C. et al. // Bioorg. Med. Chem. Lett. 2010. V. 20. № 16. P. 4771.
Brunhofer G., Studenik C., Ecker G.F. et al. // Eur. J. Pharm. Sci. 2011. V. 42. № 1–2. P. 37.
Shimotori Y., Hoshi M., Ogawa N. et al. // Heterocycl. Commun. 2020. V. 26. P. 84.
Регистр лекарственных средств России: Энциклопедия лекарств. Вып. 29 / Под ред. Вышковского Г.Л. Москва: Веданта, 2021.
Mahantaa N., Szantai-Kisc M., Peterssonc E.J. et al. // ACS Chem. Biol. 2019. V. 14. № 2. P. 142.
Vale N., Gomes P., Santos H. // Curr. Drug Metab. 2013. V. 14. № 1. P. 151.
Mills III, T., Roberson J.C. Instrumental Data for Drug Analysis. V. 2. N.Y.: Elsevier, 1992. 1577 p.
Eccles K.S., Morrison R.E., Maguire A.R. et al. // Cryst. Growth Des. 2014. V. 14. P. 2753.
Wysokinski R., Michalska D., Bienko D.C. et al. // J. Mol. Struct. 2006. V. 791. № 1–3. P. 70.
Vale N., Makila E., Salonen J. et al. // Eur. J. Pharm. Biopharm. 2012. V. 81. P. 314.
Sanina N.A., Starostina A.A., Utenyshev A.N. et al. // Molecules. 2022. V. 27. P. 6886.
Карякин Ю.В., Ангелов И.И. Чистые химические вещества. М.: Химия, 1974. 408 с.
Sanina N.A., Aldoshin S.M., Rudneva T.N. // Russ. J. Coord. Chem. 2005. V. 31. № 5. P. 301. https://doi.org/10.1007/s11173-005-0093-3
Weissberger A., Proskauer E., Riddick J.A. et al. Organic Solvents: Physical Properties and Methods of Purification. N.Y.: Intercscience Publishers Inc., 1955. 1344 p.
Agilent. CrysAlis PRO. Yarnton–Oxfordshire (England): Agilent Technologies UK Ltd., 2011.
Sheldrick G.M. SHELXTL. Version 6.14. Structure Determination Software Suite. Madison (WI, USA): Bruker AXS, 2000.
МУК 4.2.1890–04. Определение чувствительности микроорганизмов к антибактериальным препаратам. Методические указания: дата введения 2014-03-04. М.: Федеральный центр госсанэпиднадзора Минздрава России, 2004. 91 с.
Либинзон Р.Е., Щеколдина Т.Г., Батолкина О.Е. и др. // Вопросы медицинской химии. 1977. 23. № 4. С. 526.
Татьяненко Л.В., Котельников А.И., Доброхотова О.В. и др. // Хим.-фарм. журн. 2009. Т. 43. № 9. С. 45.
Березин И.В., Клесов А.А. Практический курс химической и ферментативной кинетики. М.: Изд-во Моск. ун-та, 1976. 324 с.
Glidewell C., Hursthouse M.B., Lambert R.J. et al. // Dalton Trans. 1989. P. 2061.
Sanina N.A., Rakova O.A., Aldoshin S.M. et al. // Russ. J. Coord. Chem. 2001. V. 27. № 3. P. 179. https://doi.org/10.1023/A:1009598228585
Sanina N.A., Emel’yanova N.S., Chekhlov A.N. et al. // Russ. Chem. Bull. 2010. V. 59. P. 1126.
Sanina N.A., Sulimenkov I.V., Rudneva T.N. et al. // Dokl. Chem. 2009. V. 425. Pt 1. P. 60.
Chan C., Hardin T.C., Smart J.I. // Future Microbiol. 2015. V. 10. P. 1325.
Omori K., Kotera J. // Circ. Res. 2007. V. 100. P. 309.
Hardman J.G., Robison G.A., Sutherland E.W. // Annu. Rev. Physiol. 1971. V. 33. P. 311.
Padda I.S., Tripp J. Phosphodiesterase Inhibitors. Treasure Island (FL): StatPearls Publishing LLC, 2022.
Baillie G.S., Tejeda G.S., Kelly M.P. // Nat. Rev. Drug Discov. 2019. V. 18. P. 770.
Miller M.S. // J. Receptor, Ligand Channel Res. 2015. V. 8. P. 19.