Мақаланы E-mail арқылы жіберу Development of a New Inhibitor of Bacterial Cystathionine γ-Lyase Based on 6-Bromoindole and Aminothiophene
- Авторлар: Novikov R.A.1,2, Platonov D.N.2, Bely A.Y.2, Potapov K.V.1,2, Novikov M.A.1,2, Tomilov Y.V.2, Kechko O.I.1, Seregina T.A.1, Solyev P.N.1, Mitkevich V.A.1
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Мекемелер:
- Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences
- Zelinsky Institute of Organic Chemistry of the Russian Academy of Sciences
- Шығарылым: Том 58, № 6 (2024)
- Беттер: 975-982
- Бөлім: ПОЛУЧЕНИЕ И СТРУКТУРНО-ФУНКЦИОНАЛЬНЫЙ АНАЛИЗ ПРОТИВОМИКРОБНЫХ СРЕДСТВ
- URL: https://innoscience.ru/0026-8984/article/view/677886
- DOI: https://doi.org/10.31857/S0026898424060083
- EDN: https://elibrary.ru/IAYTTU
- ID: 677886
Дәйексөз келтіру
Ашық рұқсат
Рұқсат берілді
Аннотация
Cystathionine γ-lyase (CSE) is a key enzyme for the H2S generation in such pathogenic bacteria as Staphylococcus aureus, Pseudomonas aeruginosa, etc. Suppression of CSE activity significantly increases the sensitivity of bacteria to the action of antibiotics. Here, we present a method for the synthesis of a novel indole-based CSE inhibitor, 3-amino-5-[(6-bromo-1H-indol-1-yl)methyl]thiophene, named MNS1. The synthesis of this compound is based on the modification of substituted thiophene as the main structural fragment, which is involved the alkylation of 6-bromoindole at the final stages. The dissociation constant of the MNS1 complex with bacterial CSE (from S. aureus, SaCSE) was 0.5 μM, which was an order of magnitude lower than that for human CSE (hCSE). The MNS1 compound was shown to effectively enhance the antibacterial effect of gentamicin against Bacillus subtilis, allowing it to be used as an antibiotic potentiator, to inhibit the growth of CSE-expressing bacterial cells.
Негізгі сөздер
Толық мәтін
Авторлар туралы
R. Novikov
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences; Zelinsky Institute of Organic Chemistry of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991; Moscow, 119991
D. Platonov
Zelinsky Institute of Organic Chemistry of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991
A. Bely
Zelinsky Institute of Organic Chemistry of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991
K. Potapov
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences; Zelinsky Institute of Organic Chemistry of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991; Moscow, 119991
M. Novikov
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences; Zelinsky Institute of Organic Chemistry of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991; Moscow, 119991
Yu. Tomilov
Zelinsky Institute of Organic Chemistry of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991
O. Kechko
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991
T. Seregina
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991
P. Solyev
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences
Хат алмасуға жауапты Автор.
Email: solyev@gmail.com
Ресей, Moscow, 119991
V. Mitkevich
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences
Email: solyev@gmail.com
Ресей, Moscow, 119991
Әдебиет тізімі
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