Screening of electrophilic compounds yields an aziridinyl peptide as new active-site directed SARS-CoV main protease inhibitor.
Identifieur interne : 002504 ( PubMed/Checkpoint ); précédent : 002503; suivant : 002505Screening of electrophilic compounds yields an aziridinyl peptide as new active-site directed SARS-CoV main protease inhibitor.
Auteurs : Erika Martina [Allemagne] ; Nikolaus Stiefl ; Björn Degel ; Franziska Schulz ; Alexander Breuning ; Markus Schiller ; Radim Vicik ; Knut Baumann ; John Ziebuhr ; Tanja SchirmeisterSource :
- Bioorganic & medicinal chemistry letters [ 0960-894X ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Cysteine endopeptidases, Protéines virales.
- pharmacologie : Aziridines, Inhibiteurs de protéases, Peptides.
- traitement médicamenteux : Syndrome respiratoire aigu sévère.
- Humains, Sites de fixation, Virus du SRAS.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- chemical , pharmacology : Aziridines, Peptides, Protease Inhibitors.
- drug effects : SARS Virus.
- drug therapy : Severe Acute Respiratory Syndrome.
- Binding Sites, Humans.
Abstract
The coronavirus main protease, M(pro), is considered a major target for drugs suitable to combat coronavirus infections including the severe acute respiratory syndrome (SARS). In this study, comprehensive HPLC- and FRET-substrate-based screenings of various electrophilic compounds were performed to identify potential M(pro) inhibitors. The data revealed that the coronaviral main protease is inhibited by aziridine- and oxirane-2-carboxylates. Among the trans-configured aziridine-2,3-dicarboxylates the Gly-Gly-containing peptide 2c was found to be the most potent inhibitor.
DOI: 10.1016/j.bmcl.2005.09.012
PubMed: 16216498
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:16216498Le document en format XML
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<front><div type="abstract" xml:lang="en">The coronavirus main protease, M(pro), is considered a major target for drugs suitable to combat coronavirus infections including the severe acute respiratory syndrome (SARS). In this study, comprehensive HPLC- and FRET-substrate-based screenings of various electrophilic compounds were performed to identify potential M(pro) inhibitors. The data revealed that the coronaviral main protease is inhibited by aziridine- and oxirane-2-carboxylates. Among the trans-configured aziridine-2,3-dicarboxylates the Gly-Gly-containing peptide 2c was found to be the most potent inhibitor.</div>
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<name sortKey="Breuning, Alexander" sort="Breuning, Alexander" uniqKey="Breuning A" first="Alexander" last="Breuning">Alexander Breuning</name>
<name sortKey="Degel, Bjorn" sort="Degel, Bjorn" uniqKey="Degel B" first="Björn" last="Degel">Björn Degel</name>
<name sortKey="Schiller, Markus" sort="Schiller, Markus" uniqKey="Schiller M" first="Markus" last="Schiller">Markus Schiller</name>
<name sortKey="Schirmeister, Tanja" sort="Schirmeister, Tanja" uniqKey="Schirmeister T" first="Tanja" last="Schirmeister">Tanja Schirmeister</name>
<name sortKey="Schulz, Franziska" sort="Schulz, Franziska" uniqKey="Schulz F" first="Franziska" last="Schulz">Franziska Schulz</name>
<name sortKey="Stiefl, Nikolaus" sort="Stiefl, Nikolaus" uniqKey="Stiefl N" first="Nikolaus" last="Stiefl">Nikolaus Stiefl</name>
<name sortKey="Vicik, Radim" sort="Vicik, Radim" uniqKey="Vicik R" first="Radim" last="Vicik">Radim Vicik</name>
<name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name>
</noCountry>
<country name="Allemagne"><noRegion><name sortKey="Martina, Erika" sort="Martina, Erika" uniqKey="Martina E" first="Erika" last="Martina">Erika Martina</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
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