|
ИСТИНА |
Войти в систему Регистрация |
ИПМех РАН |
||
Design of an Activity-Based Probe for Human Neutrophil Elastase: Implementation of the Lossen Rearrangement To Induce Förster Resonance Energy Transfersстатья
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: 10 августа 2018 г.
- Авторы: Anna-Christina Schulz-Fincke, Tikhomirov Alexander S., Annett Braune, Tamara Girbl, Erik Gilberg, Jürgen Bajorath, Michael Blaut, Sussan Nourshargh, Michael Gütschow
- Журнал: Biochemistry
- Том: 57
- Год издания: 2018
- Издательство: American Chemical Society
- Местоположение издательства: United States
- Первая страница: 742
- Последняя страница: 752
- DOI: 10.1021/acs.biochem.7b00906
- Аннотация: Human neutrophil elastase is an important regulator of the immune response and plays a role in host defense mechanisms and further physiological processes. The uncontrolled activity of this serine protease may cause severe tissue alterations and impair inflammatory states. The design of an activity-based probe for human neutrophil elastase reported herein relies on a sulfonyloxyphthalimide moiety as a new type of warhead that is linker-connected to a coumarin fluorophore. The inhibitory potency of the activity-based probe was assessed against several serine and cysteine proteases, and the selectivity for human neutrophil elastase (Ki = 6.85 nM) was determined. The adequate fluorescent tag of the probe allowed for the in-gel fluorescence detection of human neutrophil elastase in the low nanomolar range. The coumarin moiety and the anthranilic acid function of the probe, produced in the course of a Lossen rearrangement, were part of two different Förster resonance energy transfers.
- Добавил в систему: Тихомиров Александр Сергеевич