Isoxazol-5(2H)-one: a new scaffold for potent human neutrophil elastase (HNE) inhibitors; Journal of Enzyme Inhibition and Medicinal Chemistry; Vol. 32, iss. 1

Dades bibliogràfiques
Parent link:Journal of Enzyme Inhibition and Medicinal Chemistry
Vol. 32, iss. 1.— 2017.— [P. 821-831]
Autor corporatiu: Национальный исследовательский Томский политехнический университет (ТПУ) Институт физики высоких технологий (ИФВТ) Кафедра биотехнологии и органической химии (БИОХ)
Altres autors: Vergelli C. Claudia, Schepetkin (Shchepyotkin) I. A. Igor Aleksandrovich, Crocetti L. Letizia, Iacovone A. Antonella, Giovannoni M. P. Maria Paola, Guerrini G. Gabriella, Khlebnikov A. I. Andrey Ivanovich, Ciattini S. Samuele, Ciciani G. Giovanna, Quinn M. T. Mark
Sumari:Title screen
Human neutrophil elastase (HNE) is an important target for the development of novel and selective inhibitors to treat inflammatory diseases, especially pulmonary pathologies. Here, we report the synthesis, structure-activity relationship analysis, and biological evaluation of a new series of HNE inhibitors with an isoxazol-5(2H)-one scaffold. The most potent compound (2o) had a good balance between HNE inhibitory activity (IC50value =20 nM) and chemical stability in aqueous buffer (t1/2=8.9 h). Analysis of reaction kinetics revealed that the most potent isoxazolone derivatives were reversible competitive inhibitors of HNE. Furthermore, since compounds 2o and 2s contain two carbonyl groups (2-N-CO and 5-CO) as possible points of attack for Ser195, the amino acid of the active site responsible for the nucleophilic attack, docking studies allowed us to clarify the different roles played by these groups.
Режим доступа: по договору с организацией-держателем ресурса
Idioma:anglès
Publicat: 2017
Matèries:
Accés en línia:https://doi.org/10.1080/14756366.2017.1326915
Format: Electrònic Capítol de llibre
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=656791