1H-pyrrolo[2,3-b]pyridine: A new scaffold for human neutrophil elastase (HNE) inhibitors; Bioorganic & Medicinal Chemistry; Vol. 26, Iss. 21

Bibliografiske detaljer
Parent link:Bioorganic & Medicinal Chemistry
Vol. 26, Iss. 21.— 2018.— [P. 5583-5595]
Institution som forfatter: Национальный исследовательский Томский политехнический университет Инженерная школа новых производственных технологий Научно-образовательный центр Н. М. Кижнера
Andre forfattere: Crocetti L. Letizia, Giovannoni M. P. Maria Paola, Shchepyotkin I. A. Igor Aleksandrovich, Quinn M. Mark, Khlebnikov A. I. Andrey Ivanovich, Cantini N. Niccolo, Guerrini G. Gabriella, Iacovone A. Antonella, Teodori E. Elisabetta, Vergelli C. Claudia
Summary:Title screen
Human neutrophil elastase (HNE) is a potent serine protease belonging to the chymotrypsin family. It is an important target for the development of novel and selective inhibitors for the treatment of inflammatory diseases, especially pulmonary pathologies. Here, we report the synthesis and biological evaluation of a new series of HNE inhibitors with a pyrrolo[2,3-b]pyridine scaffold, which is an isomer of our previously reported indazoles, in order to assess how a shift of the nitrogen from position 2 to position 7 influences activity. The majority of new compounds were effective HNE inhibitors and had IC50 values in the micromolar/submicromolar range, with some compounds active in low nanomolar levels. For example, 2a and 2b inhibited HNE with IC50 values of 15 and 14?nM, respectively. Molecular modeling of compounds differing in the position of heteroatom(s) in the bicyclic moiety and in the oxadiazole ring demonstrated that the calculated geometries of enzyme-inhibitor complexes were in agreement with the observed biological activities. Docking experiments showed that orientation of the active pyrrolo[2,3-b]pyridines in the HNE catalytic triad Ser195-His57-Asp102 correlated with effectiveness of the inhibitor interaction with the enzyme. Thus, the pyrrolo[2,3-b]pyridine scaffold represents a novel scaffold for the development of potent HNE inhibitors.
Режим доступа: по договору с организацией-держателем ресурса
Sprog:engelsk
Udgivet: 2018
Fag:
Online adgang:https://doi.org/10.1016/j.bmc.2018.09.034
Format: Electronisk Book Chapter
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=659744

MARC

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200 1 |a 1H-pyrrolo[2,3-b]pyridine: A new scaffold for human neutrophil elastase (HNE) inhibitors  |f L. Crocetti, M. P. Giovannoni, I. A. Shchepyotkin [et al.] 
203 |a Text  |c electronic 
300 |a Title screen 
320 |a [References: 38 tit.] 
330 |a Human neutrophil elastase (HNE) is a potent serine protease belonging to the chymotrypsin family. It is an important target for the development of novel and selective inhibitors for the treatment of inflammatory diseases, especially pulmonary pathologies. Here, we report the synthesis and biological evaluation of a new series of HNE inhibitors with a pyrrolo[2,3-b]pyridine scaffold, which is an isomer of our previously reported indazoles, in order to assess how a shift of the nitrogen from position 2 to position 7 influences activity. The majority of new compounds were effective HNE inhibitors and had IC50 values in the micromolar/submicromolar range, with some compounds active in low nanomolar levels. For example, 2a and 2b inhibited HNE with IC50 values of 15 and 14?nM, respectively. Molecular modeling of compounds differing in the position of heteroatom(s) in the bicyclic moiety and in the oxadiazole ring demonstrated that the calculated geometries of enzyme-inhibitor complexes were in agreement with the observed biological activities. Docking experiments showed that orientation of the active pyrrolo[2,3-b]pyridines in the HNE catalytic triad Ser195-His57-Asp102 correlated with effectiveness of the inhibitor interaction with the enzyme. Thus, the pyrrolo[2,3-b]pyridine scaffold represents a novel scaffold for the development of potent HNE inhibitors. 
333 |a Режим доступа: по договору с организацией-держателем ресурса 
461 |t Bioorganic & Medicinal Chemistry 
463 |t Vol. 26, Iss. 21  |v [P. 5583-5595]  |d 2018 
610 1 |a электронный ресурс 
610 1 |a труды учёных ТПУ 
610 1 |a human neutrophil elastase 
610 1 |a inhibitor 
610 1 |a pyrrolo[2,3-b]pyridine 
610 1 |a molecular docking 
610 1 |a нейтрофильная фаза 
610 1 |a ингибиторы 
610 1 |a пирролы 
610 1 |a пиридин 
610 1 |a пиридины 
610 1 |a молекулярная стыковка 
701 1 |a Crocetti  |b L.  |g Letizia 
701 1 |a Giovannoni  |b M. P.  |g Maria Paola 
701 1 |a Shchepyotkin  |b I. A.  |c doctor-biophysicist  |c leading researcher of Tomsk Polytechnic University, candidate of medical science  |f 1962-  |g Igor Aleksandrovich  |3 (RuTPU)RU\TPU\pers\37358 
701 1 |a Quinn  |b M.  |g Mark 
701 1 |a Khlebnikov  |b A. I.  |c Chemist  |c Professor of Tomsk Polytechnic University  |f 1963-  |g Andrey Ivanovich  |3 (RuTPU)RU\TPU\pers\33927  |9 17500 
701 1 |a Cantini  |b N.  |g Niccolo 
701 1 |a Guerrini  |b G.  |g Gabriella 
701 1 |a Iacovone  |b A.  |g Antonella 
701 1 |a Teodori  |b E.  |g Elisabetta 
701 1 |a Vergelli  |b C.  |g Claudia 
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