Comparative Evaluation of Effectiveness of Biocatalytic Synthesis and Antibacterial Activity of Known Antibiotics and “Chimeric” Cephalosporin Compounds

Capa

Citar

Texto integral

Acesso aberto Acesso aberto
Acesso é fechado Acesso está concedido
Acesso é fechado Somente assinantes

Resumo

The processes of biocatalytic synthesis of cefamandole and cefazoline, as well as four “chimeric” cephalosporins carrying functional groups of these antibiotics in the C3 or C7 position of β-lactam, were carried out using immobilized cephalosporin-acid synthetase under mild standard conditions. A higher efficiency of biocatalytic acylation of β-lactams with a 1(H)-tetrazolylacetic acid residue compared to acylation with almond acid residue was demonstrated. The chemical structure of the obtained compounds was confirmed using the HPLC–MS method. The possibility of using directly reaction mixtures for evaluating the antibacterial activity of synthesized compounds without isolating the target products was demonstrated. The activity of the obtained cephalosporins against twelve microorganisms belonging to the genera Enterococcus, Acinetobacter, Serratia, Pseudomonas, Staphylococcus and Escherichia was evaluated by diffusion into agar. The activity of synthesized “chimeric” cephalosporins against four microorganisms was found: Escherichia coli VKPM B-6695, Staphylococcus aureus VKPM B-6646, Staphylococcus aureus VKPM B-8171 and Staphylococcus epidermidis VKPM B-12635.

Texto integral

Acesso é fechado

Sobre autores

A. Sklyarenko

National Research Center “Kurchatov Institute”

Autor responsável pela correspondência
Email: ingagrosh@mail.ru
Rússia, Moscow

I. Groshkova

National Research Center “Kurchatov Institute”

Email: ingagrosh@mail.ru
Rússia, Moscow

N. Gorbunov

National Research Center “Kurchatov Institute”

Email: ingagrosh@mail.ru
Rússia, Moscow

A. Vasiliev

National Research Center “Kurchatov Institute”

Email: ingagrosh@mail.ru
Rússia, Moscow

A. Kamaev

National Research Center “Kurchatov Institute”

Email: ingagrosh@mail.ru
Rússia, Moscow

S. Yarotsky

National Research Center “Kurchatov Institute”

Email: ingagrosh@mail.ru
Rússia, Moscow

Bibliografia

  1. Verma T., Aggarwal A., Singh S., Sharma S., Sarma S.J. // J. Mol. Struct. 2022. V. 1248. P. 1‒13. https://doi.org/10.1016/j.molstruc.2021.131380
  2. Аркуша А.А. // Скиф. 2018. T.12. № 28. C. 7–19.
  3. Сидоренко С.В., Тишков В. И. // Успехи биологической химии. 2004. T. 44. C. 263‒306.
  4. Rodriguez-Herrera R., Puc L.E.C., Sobrevilla J.M.V., Luque D., Cardona-Felix C.S., Aguilar-Conzalez C.N. et al. // In: Enzymes in Food Biotechnology – Production, Applications, and Future Prospects. / Ed. M. Kuddus. Acad. Press. 2018. V. 36. P. 627‒643. https://doi.org/10.1016/B978-0-12-813280-7.00036-0
  5. Theuretzbacher U. // Curr. Opin. Pharmacol. 2011. V. 11. № 5. P. 433‒438. https://doi.org/10.1016/j.coph.2011.07.008
  6. Gaurav K., Karmakar S., Kundu S., Кundu K. // In: Antibiotic Resistant Bacteria – A Continuous Challenge in the New Millennium. / Ed. Dr. Marina Pana. InTech. 2012. P. 487‒502. https://doi.org/10.5772/29658
  7. Kurochkina V.B., Satarova D.E., Nys P.S. Moscow University Chemistry Bulletin. Biocatalysis. 2000. V. 41. № 6. Р. 139‒143.
  8. Курочкина В.Б., Ныс П.С. // Антибиотики и химиотерапия. 2002. № 2. С. 29‒37.
  9. Sklyarenko A.V., Groshkova I.A., Gorbunov N.A., Yarotsky S.V. // Appl. Biochem. Microbiol. 2023. T. 57. № 7. C. 1027‒1038. https://doi.org/10.1134/S0003683823070062
  10. Arroyo M., De la Mata I., García J.-L., Barredo J.-L. // Biotechnology of Microbial Enzymes. 2017. V. 17. P. 451‒473. https://doi.org/10.1016/B978-0-12-803725-6.00017-0
  11. Sklyarenko A.V., Eldarov M.A., Kurochkina V.B., Yarotsky S.V. // Appl. Biochem. Microbiol. 2015. V. 51. № 6. P. 627‒640. https://doi.org/10.1134/S0003683815060150
  12. Эльдаров М.А., Скляренко А.В., Думина М.В., Медведева Н.В., Жгун А.А., Сатарова Д.Э. и др. // Биомедицинская химия. 2015. T. 61. № 5. C. 646‒651. https://doi.org/10.18097/PBMC20156105646
  13. Sklyarenko A.V., Groshkova I.A., Sidorenko A.I., Yarotsky S.V. // Appl. Biochem. Microbiol. 2020. V. 56. № 5. P. 526‒537. https://doi.org/10.1134/S0003683820050130
  14. Sklyarenko A.V., Groshkova I.A., Krestyanova I.N., Yarotsky S.V. // Appl. Biochem. Microbiol. 2022. V. 58. № 3. P. 251‒260. https://doi.org/10.1134/S0003683822030127
  15. Sklyarenko A.V., Groshkova I.A., Gorbunov N.A., Yarotsky S.V. Appl. Biochem. Microbiol. 2023. T. 59. № 8. C. 1086‒1101. https://doi.org/10.1134/S0003683823080094
  16. Wang Lu, Sklyarenko A.V., Duanhua Li, Sidorenko A.I., Zhao C., Jinjun Li et al. // Bioprocess Biosyst. Eng. 2018. V. 41. № 12. P. 1851‒1867. https://doi.org/10.1007/s00449-018-2007-z
  17. Deaguero A.L., Blum J.K., Bommarius A.S. // In: Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation, and Cell Technology. / Ed. M. C. Flickinger. John Wiley & Sons, 2012. P. 535‒567. https://doi.org/10.1002/9780470054581.eib640
  18. Кулешова С.И. // Ведомости Научного центра экспертизы средств медицинского применения. 2015. (3). C. 13‒17.
  19. Kurochkina V.B., Sklyarenko A.V. // In: Biotechnology: State of the Art and Prospects for Development / Ed. G.E. Zaikov. Nova Science Publishers, 2008. V. 20. P. 175‒204.

Arquivos suplementares

Arquivos suplementares
Ação
1. JATS XML
Baixar
2. Fig. 1. Scheme of kinetically controlled synthesis of cephalosporins.

Baixar (14KB)
Metadados
3. Fig. 2. Accumulation curves of cephalosporins during synthesis using the IECASA biocatalyst: 1 – CFM (7-TMCA_МА), 2 – S-p CFM (7-ACA_МА), 3 – Chimera (TDA_МА), 4 – CEZ (TDA_TzAA), 5 – Sp-CEZ (7-ACA_TzAA), 6 – Chimera (7-TMCA_TzAA). The formulas of cephalosporins are given in Table 2.

Baixar (18KB)
Metadados
4. Table 1.1

Baixar (891B)
Metadados
5. Table 1.2

Baixar (269B)
Metadados
6. Table 1.3

Baixar (375B)
Metadados
7. Table 1.4

Baixar (261B)
Metadados
8. Table 1.5

Baixar (219B)
Metadados
9. Table 1.6

Baixar (267B)
Metadados
10. Table 1.7

Baixar (356B)
Metadados
11. Table 1.8

Baixar (299B)
Metadados
12. Table 1.9

Baixar (360B)
Metadados
13. Table 1.10

Baixar (286B)
Metadados
14. Table 1.11

Baixar (216B)
Metadados
15. Table 1.12

Baixar (300B)
Metadados
16. Table 1.13

Baixar (358B)
Metadados
17. Table 2.1

Baixar (836B)
Metadados
18. Table 2.2

Baixar (701B)
Metadados
19. Table 2.3

Baixar (754B)
Metadados
20. Table 2.4

Baixar (790B)
Metadados
21. Table 2.5

Baixar (786B)
Metadados
22. Table 2.6

Baixar (894B)
Metadados

Declaração de direitos autorais © Russian Academy of Sciences, 2024