Inhibition of SARS-CoV 3CL protease by flavonoids.
Identifieur interne : 000860 ( PubMed/Curation ); précédent : 000859; suivant : 000861Inhibition of SARS-CoV 3CL protease by flavonoids.
Auteurs : Seri Jo [Corée du Sud] ; Suwon Kim [Corée du Sud] ; Dong Hae Shin [Corée du Sud] ; Mi-Sun Kim [Corée du Sud]Source :
- Journal of enzyme inhibition and medicinal chemistry [ 1475-6374 ] ; 2020.
Descripteurs français
- KwdFr :
- Antienzymes (), Antienzymes (pharmacologie), Antienzymes (synthèse chimique), Antiviraux (), Antiviraux (pharmacologie), Antiviraux (synthèse chimique), Cysteine endopeptidases (isolement et purification), Cysteine endopeptidases (métabolisme), Flavonoïdes (), Flavonoïdes (pharmacologie), Flavonoïdes (synthèse chimique), Humains, Protéines virales (antagonistes et inhibiteurs), Protéines virales (isolement et purification), Protéines virales (métabolisme), Relation dose-effet des médicaments, Relation structure-activité, Structure moléculaire, Virus du SRAS (), Virus du SRAS (enzymologie).
- MESH :
- antagonistes et inhibiteurs : Protéines virales.
- enzymologie : Virus du SRAS.
- isolement et purification : Cysteine endopeptidases, Protéines virales.
- métabolisme : Cysteine endopeptidases, Protéines virales.
- pharmacologie : Antienzymes, Antiviraux, Flavonoïdes.
- synthèse chimique : Antienzymes, Antiviraux, Flavonoïdes.
- Antienzymes, Antiviraux, Flavonoïdes, Humains, Relation dose-effet des médicaments, Relation structure-activité, Structure moléculaire, Virus du SRAS.
English descriptors
- KwdEn :
- Antiviral Agents (chemical synthesis), Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Cysteine Endopeptidases (isolation & purification), Cysteine Endopeptidases (metabolism), Dose-Response Relationship, Drug, Enzyme Inhibitors (chemical synthesis), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (pharmacology), Flavonoids (chemical synthesis), Flavonoids (chemistry), Flavonoids (pharmacology), Humans, Molecular Structure, SARS Virus (drug effects), SARS Virus (enzymology), Structure-Activity Relationship, Viral Proteins (antagonists & inhibitors), Viral Proteins (isolation & purification), Viral Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Viral Proteins.
- chemical , chemical synthesis : Antiviral Agents, Enzyme Inhibitors, Flavonoids.
- chemical , chemistry : Antiviral Agents, Enzyme Inhibitors, Flavonoids.
- chemical , isolation & purification : Cysteine Endopeptidases, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- chemical , pharmacology : Antiviral Agents, Enzyme Inhibitors, Flavonoids.
- drug effects : SARS Virus.
- enzymology : SARS Virus.
- Dose-Response Relationship, Drug, Humans, Molecular Structure, Structure-Activity Relationship.
Abstract
There were severe panics caused by Severe Acute Respiratory Syndrome (SARS) and Middle-East Respiratory Syndrome-Coronavirus. Therefore, researches targeting these viruses have been required. Coronaviruses (CoVs) have been rising targets of some flavonoids. The antiviral activity of some flavonoids against CoVs is presumed directly caused by inhibiting 3C-like protease (3CLpro). Here, we applied a flavonoid library to systematically probe inhibitory compounds against SARS-CoV 3CLpro. Herbacetin, rhoifolin and pectolinarin were found to efficiently block the enzymatic activity of SARS-CoV 3CLpro. The interaction of the three flavonoids was confirmed using a tryptophan-based fluorescence method, too. An induced-fit docking analysis indicated that S1, S2 and S3' sites are involved in binding with flavonoids. The comparison with previous studies showed that Triton X-100 played a critical role in objecting false positive or overestimated inhibitory activity of flavonoids. With the systematic analysis, the three flavonoids are suggested to be templates to design functionally improved inhibitors.
DOI: 10.1080/14756366.2019.1690480
PubMed: 31724441
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pubmed:31724441Le document en format XML
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Therefore, researches targeting these viruses have been required. Coronaviruses (CoVs) have been rising targets of some flavonoids. The antiviral activity of some flavonoids against CoVs is presumed directly caused by inhibiting 3C-like protease (3CLpro). Here, we applied a flavonoid library to systematically probe inhibitory compounds against SARS-CoV 3CLpro. Herbacetin, rhoifolin and pectolinarin were found to efficiently block the enzymatic activity of SARS-CoV 3CLpro. The interaction of the three flavonoids was confirmed using a tryptophan-based fluorescence method, too. An induced-fit docking analysis indicated that S1, S2 and S3' sites are involved in binding with flavonoids. The comparison with previous studies showed that Triton X-100 played a critical role in objecting false positive or overestimated inhibitory activity of flavonoids. With the systematic analysis, the three flavonoids are suggested to be templates to design functionally improved inhibitors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31724441</PMID><DateCompleted><Year>2020</Year><Month>01</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1475-6374</ISSN><JournalIssue CitedMedium="Internet"><Volume>35</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Journal of enzyme inhibition and medicinal chemistry</Title><ISOAbbreviation>J Enzyme Inhib Med Chem</ISOAbbreviation></Journal><ArticleTitle>Inhibition of SARS-CoV 3CL protease by flavonoids.</ArticleTitle><Pagination><MedlinePgn>145-151</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/14756366.2019.1690480</ELocationID><Abstract><AbstractText>There were severe panics caused by Severe Acute Respiratory Syndrome (SARS) and Middle-East Respiratory Syndrome-Coronavirus. Therefore, researches targeting these viruses have been required. Coronaviruses (CoVs) have been rising targets of some flavonoids. The antiviral activity of some flavonoids against CoVs is presumed directly caused by inhibiting 3C-like protease (3CLpro). Here, we applied a flavonoid library to systematically probe inhibitory compounds against SARS-CoV 3CLpro. Herbacetin, rhoifolin and pectolinarin were found to efficiently block the enzymatic activity of SARS-CoV 3CLpro. The interaction of the three flavonoids was confirmed using a tryptophan-based fluorescence method, too. An induced-fit docking analysis indicated that S1, S2 and S3' sites are involved in binding with flavonoids. The comparison with previous studies showed that Triton X-100 played a critical role in objecting false positive or overestimated inhibitory activity of flavonoids. With the systematic analysis, the three flavonoids are suggested to be templates to design functionally improved inhibitors.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jo</LastName><ForeName>Seri</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>College of Pharmacy and Graduates School of Pharmaceutical Sciences, Ewha W. University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Suwon</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>College of Pharmacy and Graduates School of Pharmaceutical Sciences, Ewha W. University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shin</LastName><ForeName>Dong Hae</ForeName><Initials>DH</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-2205-1453</Identifier><AffiliationInfo><Affiliation>College of Pharmacy and Graduates School of Pharmaceutical Sciences, Ewha W. University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Mi-Sun</ForeName><Initials>MS</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-4092-4203</Identifier><AffiliationInfo><Affiliation>College of Pharmacy and Graduates School of Pharmaceutical Sciences, Ewha W. University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Enzyme Inhib Med Chem</MedlineTA><NlmUniqueID>101150203</NlmUniqueID><ISSNLinking>1475-6366</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005419">Flavonoids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="C099456">3C-like proteinase, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005419" MajorTopicYN="N">Flavonoids</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">FRET</Keyword><Keyword MajorTopicYN="N">SARS-CoV</Keyword><Keyword MajorTopicYN="N">SARS-CoV 3CLpro</Keyword><Keyword MajorTopicYN="N">flavonoid</Keyword><Keyword MajorTopicYN="N">inhibitory compounds</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate 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| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |