Screening and evaluation of approved drugs as inhibitors of main protease of SARS-CoV-2.
Identifieur interne : 000D72 ( Main/Corpus ); précédent : 000D71; suivant : 000D73Screening and evaluation of approved drugs as inhibitors of main protease of SARS-CoV-2.
Auteurs : Praveen Kumar Tripathi ; Saurabh Upadhyay ; Manju Singh ; Siva Raghavendhar ; Mohit Bhardwaj ; Pradeep Sharma ; Ashok Kumar PatelSource :
- International journal of biological macromolecules [ 1879-0003 ] ; 2020.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Betacoronavirus (drug effects), Betacoronavirus (enzymology), Betacoronavirus (physiology), COVID-19 (MeSH), Coronavirus 3C Proteases (MeSH), Coronavirus Infections (drug therapy), Coronavirus Infections (virology), Cysteine Endopeptidases (MeSH), Drug Evaluation, Preclinical (methods), Drug Repositioning (methods), Humans (MeSH), Molecular Docking Simulation (MeSH), Pandemics (MeSH), Pneumonia, Viral (drug therapy), Pneumonia, Viral (virology), Protease Inhibitors (chemistry), Protease Inhibitors (pharmacology), SARS-CoV-2 (MeSH), Teicoplanin (chemistry), Teicoplanin (pharmacology), Viral Nonstructural Proteins (antagonists & inhibitors), Virus Replication (drug effects).
- MESH :
- chemical , antagonists & inhibitors : Viral Nonstructural Proteins.
- chemical , chemistry : Antiviral Agents, Protease Inhibitors, Teicoplanin.
- chemical , pharmacology : Antiviral Agents, Protease Inhibitors, Teicoplanin.
- drug effects : Betacoronavirus, Virus Replication.
- drug therapy : Coronavirus Infections, Pneumonia, Viral.
- enzymology : Betacoronavirus.
- methods : Drug Evaluation, Preclinical, Drug Repositioning.
- physiology : Betacoronavirus.
- virology : Coronavirus Infections, Pneumonia, Viral.
- Amino Acid Sequence, COVID-19, Coronavirus 3C Proteases, Cysteine Endopeptidases, Humans, Molecular Docking Simulation, Pandemics, SARS-CoV-2.
Abstract
The COVID-19 pandemic caused by SARS-CoV-2 has emerged as a global catastrophe. The virus requires main protease for processing the viral polyproteins PP1A and PP1AB translated from the viral RNA. In search of a quick, safe and successful therapeutic agent; we screened various clinically approved drugs for the in-vitro inhibitory effect on 3CLPro which may be able to halt virus replication. The methods used includes protease activity assay, fluorescence quenching, surface plasmon resonance (SPR), Thermofluor® Assay, Size exclusion chromatography and in-silico docking studies. We found that Teicoplanin as most effective drug with IC50 ~ 1.5 μM. Additionally, through fluorescence quenching Stern-Volmer quenching constant (KSV) for Teicoplanin was estimated as 2.5 × 105 L·mol-1, which suggests a relatively high affinity between Teicoplanin and 3CLPro protease. The SPR shows good interaction between Teicoplanin and 3CLPro with KD ~ 1.6 μM. Our results provide critical insights into the mechanism of action of Teicoplanin as a potential therapeutic against COVID-19. We found that Teicoplanin is about 10-20 fold more potent in inhibiting protease activity than other drugs in use, such as lopinavir, hydroxychloroquine, chloroquine, azithromycin, atazanavir etc. Therefore, Teicoplanin emerged as the best inhibitor among all drug molecules we screened against 3CLPro of SARS-CoV-2.
DOI: 10.1016/j.ijbiomac.2020.08.166
PubMed: 32853604
PubMed Central: PMC7444494
Links to Exploration step
pubmed:32853604Le document en format XML
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Electronic address: ashokpatel@bioschool.iitd.ac.in.</nlm:affiliation></affiliation></author></analytic><series><title level="j">International journal of biological macromolecules</title><idno type="eISSN">1879-0003</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Antiviral Agents (chemistry)</term><term>Antiviral Agents (pharmacology)</term><term>Betacoronavirus (drug effects)</term><term>Betacoronavirus (enzymology)</term><term>Betacoronavirus (physiology)</term><term>COVID-19 (MeSH)</term><term>Coronavirus 3C Proteases (MeSH)</term><term>Coronavirus Infections (drug therapy)</term><term>Coronavirus Infections (virology)</term><term>Cysteine Endopeptidases (MeSH)</term><term>Drug Evaluation, Preclinical (methods)</term><term>Drug Repositioning (methods)</term><term>Humans (MeSH)</term><term>Molecular Docking Simulation (MeSH)</term><term>Pandemics (MeSH)</term><term>Pneumonia, Viral (drug therapy)</term><term>Pneumonia, Viral (virology)</term><term>Protease Inhibitors (chemistry)</term><term>Protease Inhibitors (pharmacology)</term><term>SARS-CoV-2 (MeSH)</term><term>Teicoplanin (chemistry)</term><term>Teicoplanin (pharmacology)</term><term>Viral Nonstructural Proteins (antagonists & inhibitors)</term><term>Virus Replication (drug effects)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term><term>Protease Inhibitors</term><term>Teicoplanin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Protease Inhibitors</term><term>Teicoplanin</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Betacoronavirus</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Coronavirus Infections</term><term>Pneumonia, Viral</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Betacoronavirus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Evaluation, Preclinical</term><term>Drug Repositioning</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Betacoronavirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term><term>Pneumonia, Viral</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>COVID-19</term><term>Coronavirus 3C Proteases</term><term>Cysteine Endopeptidases</term><term>Humans</term><term>Molecular Docking Simulation</term><term>Pandemics</term><term>SARS-CoV-2</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The COVID-19 pandemic caused by SARS-CoV-2 has emerged as a global catastrophe. The virus requires main protease for processing the viral polyproteins PP1A and PP1AB translated from the viral RNA. In search of a quick, safe and successful therapeutic agent; we screened various clinically approved drugs for the in-vitro inhibitory effect on 3CL<sup>Pro</sup> which may be able to halt virus replication. The methods used includes protease activity assay, fluorescence quenching, surface plasmon resonance (SPR), Thermofluor® Assay, Size exclusion chromatography and in-silico docking studies. We found that Teicoplanin as most effective drug with IC<sub>50</sub> ~ 1.5 μM. Additionally, through fluorescence quenching Stern-Volmer quenching constant (K<sub>SV</sub>) for Teicoplanin was estimated as 2.5 × 10<sup>5</sup> L·mol<sup>-1</sup>, which suggests a relatively high affinity between Teicoplanin and 3CL<sup>Pro</sup> protease. The SPR shows good interaction between Teicoplanin and 3CL<sup>Pro</sup> with K<sub>D</sub> ~ 1.6 μM. Our results provide critical insights into the mechanism of action of Teicoplanin as a potential therapeutic against COVID-19. We found that Teicoplanin is about 10-20 fold more potent in inhibiting protease activity than other drugs in use, such as lopinavir, hydroxychloroquine, chloroquine, azithromycin, atazanavir etc. Therefore, Teicoplanin emerged as the best inhibitor among all drug molecules we screened against 3CL<sup>Pro</sup> of SARS-CoV-2.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32853604</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>23</Day></DateCompleted><DateRevised><Year>2021</Year><Month>01</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>164</Volume><PubDate><Year>2020</Year><Month>Dec</Month><Day>01</Day></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int J Biol Macromol</ISOAbbreviation></Journal><ArticleTitle>Screening and evaluation of approved drugs as inhibitors of main protease of SARS-CoV-2.</ArticleTitle><Pagination><MedlinePgn>2622-2631</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(20)34257-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2020.08.166</ELocationID><Abstract><AbstractText>The COVID-19 pandemic caused by SARS-CoV-2 has emerged as a global catastrophe. The virus requires main protease for processing the viral polyproteins PP1A and PP1AB translated from the viral RNA. In search of a quick, safe and successful therapeutic agent; we screened various clinically approved drugs for the in-vitro inhibitory effect on 3CL<sup>Pro</sup> which may be able to halt virus replication. The methods used includes protease activity assay, fluorescence quenching, surface plasmon resonance (SPR), Thermofluor® Assay, Size exclusion chromatography and in-silico docking studies. We found that Teicoplanin as most effective drug with IC<sub>50</sub> ~ 1.5 μM. Additionally, through fluorescence quenching Stern-Volmer quenching constant (K<sub>SV</sub>) for Teicoplanin was estimated as 2.5 × 10<sup>5</sup> L·mol<sup>-1</sup>, which suggests a relatively high affinity between Teicoplanin and 3CL<sup>Pro</sup> protease. The SPR shows good interaction between Teicoplanin and 3CL<sup>Pro</sup> with K<sub>D</sub> ~ 1.6 μM. Our results provide critical insights into the mechanism of action of Teicoplanin as a potential therapeutic against COVID-19. We found that Teicoplanin is about 10-20 fold more potent in inhibiting protease activity than other drugs in use, such as lopinavir, hydroxychloroquine, chloroquine, azithromycin, atazanavir etc. Therefore, Teicoplanin emerged as the best inhibitor among all drug molecules we screened against 3CL<sup>Pro</sup> of SARS-CoV-2.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tripathi</LastName><ForeName>Praveen Kumar</ForeName><Initials>PK</Initials><AffiliationInfo><Affiliation>Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, 110016, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Upadhyay</LastName><ForeName>Saurabh</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, 110016, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Singh</LastName><ForeName>Manju</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Morarji Desai National Institute of Yoga, New Delhi 110 001, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Raghavendhar</LastName><ForeName>Siva</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, 110016, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhardwaj</LastName><ForeName>Mohit</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, 110016, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sharma</LastName><ForeName>Pradeep</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Biophysics, All India Institute of Medical Sciences, Ansari Nagar, New Delhi 110029, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Patel</LastName><ForeName>Ashok Kumar</ForeName><Initials>AK</Initials><AffiliationInfo><Affiliation>Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, 110016, India. Electronic address: ashokpatel@bioschool.iitd.ac.in.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>08</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biol Macromol</MedlineTA><NlmUniqueID>7909578</NlmUniqueID><ISSNLinking>0141-8130</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>61036-62-2</RegistryNumber><NameOfSubstance UI="D017334">Teicoplanin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.28</RegistryNumber><NameOfSubstance UI="D000086782">Coronavirus 3C Proteases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000073640" MajorTopicYN="N">Betacoronavirus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000086382" MajorTopicYN="N">COVID-19</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000086782" MajorTopicYN="N">Coronavirus 3C Proteases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004353" MajorTopicYN="N">Drug Evaluation, Preclinical</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058492" MajorTopicYN="N">Drug Repositioning</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D062105" MajorTopicYN="N">Molecular Docking Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058873" MajorTopicYN="N">Pandemics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011024" MajorTopicYN="N">Pneumonia, Viral</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000086402" MajorTopicYN="N">SARS-CoV-2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017334" MajorTopicYN="N">Teicoplanin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014779" MajorTopicYN="N">Virus Replication</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">3CL-protease</Keyword><Keyword MajorTopicYN="N">Activity inhibition</Keyword><Keyword MajorTopicYN="N">Drug repurposing</Keyword></KeywordList><CoiStatement>Declaration of competing interest Authors declare no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>05</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>08</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>08</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>8</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>8</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32853604</ArticleId><ArticleId IdType="pii">S0141-8130(20)34257-4</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2020.08.166</ArticleId><ArticleId 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