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Bisbenzimidazole derivatives as potent inhibitors of the trypsin-like sites of the immunoproteasome core particleстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 2 апреля 2015 г.
- Авторы: Koroleva O.N., The Hien Pham, Bouvier D., Dufau L., Reboud-Ravaux L.Qin M, Ivanov A.A., Zhuze A.L., Gromova E.S., Bouvier-Durand M.
- Журнал: Biochimie
- Том: 108
- Номер: 1
- Год издания: 2015
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 94
- Последняя страница: 100
- DOI: 10.1016/j.biochi.2014.11.002
- Аннотация: In this study, a monomeric (MB) and a dimeric (DB) bisbenzimidazoles were identified as novel proteasome inhibitors of the trypsin-like activity located on b2c sites of the constitutive 20S proteasome (IC50 values at 2-4 mkM range). Remarkably, they were further shown to be 100- and 200-fold more potent inhibitors of the immunoproteasome trypsin-like activity (b2i sites, IC50 24 nM) than of the homologous constitutive activity. Molecular models of inhibitor/enzyme complexes in the two types of trypsin-like sites and corresponding computed binding energy values corroborated kinetic data. Different binding modes were suggested for MB and DB to the b2c and b2i trypsic sites. Each pointed to better contacts of the ligand inside the b2i active site than for b2c site. MB and DB represent the first selective inhibitors of the immunoproteasome trypsin-like activity described to date and can be considered as prototypes for inhibiting this activity.
- Добавил в систему: Громова Елизавета Сергеевна
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | 1-s2.0-S0300908414003319-main.pdf | 1-s2.0-S0300908414003319-main.pdf | 1,3 МБ | 14 сентября 2017 [olkoroleva58] |