Combination and tricombination therapy to destabilize the structural integrity of COVID-19 by some bioactive compounds with antiviral drugs: insights from molecular docking study.
Identifieur interne : 000500 ( Main/Corpus ); précédent : 000499; suivant : 000501Combination and tricombination therapy to destabilize the structural integrity of COVID-19 by some bioactive compounds with antiviral drugs: insights from molecular docking study.
Auteurs : H R Abd El-Mageed ; Doaa A. Abdelrheem ; Shimaa A. Ahmed ; Aziz A. Rahman ; Khaled N M. Elsayed ; Sayed A. Ahmed ; Ashraf A. El-Bassuony ; Hussein S. MohamedSource :
- Structural chemistry [ 1040-0400 ] ; 2021.
Abstract
Recently, the SARS-CoV-2 (COVID-19) pandemic virus has been spreading throughout the world. Until now, no certified drugs have been discovered to efficiently inhibit the virus. The scientists are struggling to find new safe bioactive inhibitors of this deadly virus. In this study, we aim to find antagonists that may inhibit the activity of the three major viral targets: SARS-CoV-2 3-chymotrypsin-like protease (6LU7), SARS-CoV-2 spike protein (6VYB), and a host target human angiotensin-converting enzyme 2 (ACE2) receptor (1R42), which is the entry point for the viral encounter, were studied with the prospects of identifying significant drug candidate(s) against COVID-19 infection. Then, the protein stability produced score of less than 0.6 for all residues of all studied receptors. This confirmed that these receptors are extremely stable proteins, so it is very difficult to unstable the stability of these proteins through utilizing individual drugs. Hence, we studied the combination and tricombination therapy between bioactive compounds which have the best binding affinity and some antiviral drugs like chloroquine, hydroxychloroquine, azithromycin, simeprevir, baloxavir, lopinavir, and favipiravir to show the effect of combination and tricombination therapy to disrupt the stability of the three major viral targets that are mentioned previously. Also, ADMET study suggested that most of all studied bioactive compounds are safe and nontoxic compounds. All results confirmed that caulerpin can be utilized as a combination and tricombination therapy along with the studied antiviral drugs for disrupting the stability of the three major viral receptors (6LU7, 6VYB, and 1R42).
Supplementary Information
The online version contains supplementary material available at 10.1007/s11224-020-01723-5.
DOI: 10.1007/s11224-020-01723-5
PubMed: 33437137
PubMed Central: PMC7791912
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Abdelrheem</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Ahmed, Shimaa A" sort="Ahmed, Shimaa A" uniqKey="Ahmed S" first="Shimaa A" last="Ahmed">Shimaa A. Ahmed</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Rahman, Aziz A" sort="Rahman, Aziz A" uniqKey="Rahman A" first="Aziz A" last="Rahman">Aziz A. Rahman</name><affiliation><nlm:affiliation>Department of Pharmacy, University of Rajshahi, Rajshahi, Bangladesh.</nlm:affiliation></affiliation></author><author><name sortKey="Elsayed, Khaled N M" sort="Elsayed, Khaled N M" uniqKey="Elsayed K" first="Khaled N M" last="Elsayed">Khaled N M. Elsayed</name><affiliation><nlm:affiliation>Department of Botany, Faculty of Science, Beni-Suef University, Beni-Suef, Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Ahmed, Sayed A" sort="Ahmed, Sayed A" uniqKey="Ahmed S" first="Sayed A" last="Ahmed">Sayed A. Ahmed</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="El Bassuony, Ashraf A" sort="El Bassuony, Ashraf A" uniqKey="El Bassuony A" first="Ashraf A" last="El-Bassuony">Ashraf A. El-Bassuony</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Mohamed, Hussein S" sort="Mohamed, Hussein S" uniqKey="Mohamed H" first="Hussein S" last="Mohamed">Hussein S. 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Abdelrheem</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Ahmed, Shimaa A" sort="Ahmed, Shimaa A" uniqKey="Ahmed S" first="Shimaa A" last="Ahmed">Shimaa A. Ahmed</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Rahman, Aziz A" sort="Rahman, Aziz A" uniqKey="Rahman A" first="Aziz A" last="Rahman">Aziz A. Rahman</name><affiliation><nlm:affiliation>Department of Pharmacy, University of Rajshahi, Rajshahi, Bangladesh.</nlm:affiliation></affiliation></author><author><name sortKey="Elsayed, Khaled N M" sort="Elsayed, Khaled N M" uniqKey="Elsayed K" first="Khaled N M" last="Elsayed">Khaled N M. Elsayed</name><affiliation><nlm:affiliation>Department of Botany, Faculty of Science, Beni-Suef University, Beni-Suef, Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Ahmed, Sayed A" sort="Ahmed, Sayed A" uniqKey="Ahmed S" first="Sayed A" last="Ahmed">Sayed A. Ahmed</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="El Bassuony, Ashraf A" sort="El Bassuony, Ashraf A" uniqKey="El Bassuony A" first="Ashraf A" last="El-Bassuony">Ashraf A. El-Bassuony</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</nlm:affiliation></affiliation></author><author><name sortKey="Mohamed, Hussein S" sort="Mohamed, Hussein S" uniqKey="Mohamed H" first="Hussein S" last="Mohamed">Hussein S. Mohamed</name><affiliation><nlm:affiliation>Research Institute of Medicinal and Aromatic Plants (RIMAP), Beni-Suef University, Beni-Suef City, Egypt.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Structural chemistry</title><idno type="ISSN">1040-0400</idno><imprint><date when="2021" type="published">2021</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recently, the SARS-CoV-2 (COVID-19) pandemic virus has been spreading throughout the world. Until now, no certified drugs have been discovered to efficiently inhibit the virus. The scientists are struggling to find new safe bioactive inhibitors of this deadly virus. In this study, we aim to find antagonists that may inhibit the activity of the three major viral targets: SARS-CoV-2 3-chymotrypsin-like protease (6LU7), SARS-CoV-2 spike protein (6VYB), and a host target human angiotensin-converting enzyme 2 (ACE2) receptor (1R42), which is the entry point for the viral encounter, were studied with the prospects of identifying significant drug candidate(s) against COVID-19 infection. Then, the protein stability produced score of less than 0.6 for all residues of all studied receptors. This confirmed that these receptors are extremely stable proteins, so it is very difficult to unstable the stability of these proteins through utilizing individual drugs. Hence, we studied the combination and tricombination therapy between bioactive compounds which have the best binding affinity and some antiviral drugs like chloroquine, hydroxychloroquine, azithromycin, simeprevir, baloxavir, lopinavir, and favipiravir to show the effect of combination and tricombination therapy to disrupt the stability of the three major viral targets that are mentioned previously. Also, ADMET study suggested that most of all studied bioactive compounds are safe and nontoxic compounds. All results confirmed that caulerpin can be utilized as a combination and tricombination therapy along with the studied antiviral drugs for disrupting the stability of the three major viral receptors (6LU7, 6VYB, and 1R42).</div><div type="abstract" xml:lang="en"><p><b>Supplementary Information</b></p><p>The online version contains supplementary material available at 10.1007/s11224-020-01723-5.</p></div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33437137</PMID><DateRevised><Year>2021</Year><Month>01</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1040-0400</ISSN><JournalIssue CitedMedium="Print"><PubDate><Year>2021</Year><Month>Jan</Month><Day>08</Day></PubDate></JournalIssue><Title>Structural chemistry</Title><ISOAbbreviation>Struct Chem</ISOAbbreviation></Journal><ArticleTitle>Combination and tricombination therapy to destabilize the structural integrity of COVID-19 by some bioactive compounds with antiviral drugs: insights from molecular docking study.</ArticleTitle><Pagination><MedlinePgn>1-16</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11224-020-01723-5</ELocationID><Abstract><AbstractText>Recently, the SARS-CoV-2 (COVID-19) pandemic virus has been spreading throughout the world. Until now, no certified drugs have been discovered to efficiently inhibit the virus. The scientists are struggling to find new safe bioactive inhibitors of this deadly virus. In this study, we aim to find antagonists that may inhibit the activity of the three major viral targets: SARS-CoV-2 3-chymotrypsin-like protease (6LU7), SARS-CoV-2 spike protein (6VYB), and a host target human angiotensin-converting enzyme 2 (ACE2) receptor (1R42), which is the entry point for the viral encounter, were studied with the prospects of identifying significant drug candidate(s) against COVID-19 infection. Then, the protein stability produced score of less than 0.6 for all residues of all studied receptors. This confirmed that these receptors are extremely stable proteins, so it is very difficult to unstable the stability of these proteins through utilizing individual drugs. Hence, we studied the combination and tricombination therapy between bioactive compounds which have the best binding affinity and some antiviral drugs like chloroquine, hydroxychloroquine, azithromycin, simeprevir, baloxavir, lopinavir, and favipiravir to show the effect of combination and tricombination therapy to disrupt the stability of the three major viral targets that are mentioned previously. Also, ADMET study suggested that most of all studied bioactive compounds are safe and nontoxic compounds. All results confirmed that caulerpin can be utilized as a combination and tricombination therapy along with the studied antiviral drugs for disrupting the stability of the three major viral receptors (6LU7, 6VYB, and 1R42).</AbstractText><AbstractText Label="Supplementary Information" NlmCategory="UNASSIGNED">The online version contains supplementary material available at 10.1007/s11224-020-01723-5.</AbstractText><CopyrightInformation>© The Author(s), under exclusive licence to Springer Science+Business Media, LLC part of Springer Nature 2021.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>El-Mageed</LastName><ForeName>H R Abd</ForeName><Initials>HRA</Initials><AffiliationInfo><Affiliation>Micro-analysis and Environmental Research and Community Services Center, Faculty of Science, Beni-Suef University, Beni-Suef City, Egypt.</Affiliation><Identifier Source="GRID">grid.411662.6</Identifier><Identifier Source="ISNI">0000 0004 0412 4932</Identifier></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Abdelrheem</LastName><ForeName>Doaa A</ForeName><Initials>DA</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</Affiliation><Identifier Source="GRID">grid.411662.6</Identifier><Identifier Source="ISNI">0000 0004 0412 4932</Identifier></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahmed</LastName><ForeName>Shimaa A</ForeName><Initials>SA</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</Affiliation><Identifier Source="GRID">grid.411662.6</Identifier><Identifier Source="ISNI">0000 0004 0412 4932</Identifier></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rahman</LastName><ForeName>Aziz A</ForeName><Initials>AA</Initials><AffiliationInfo><Affiliation>Department of Pharmacy, University of Rajshahi, Rajshahi, Bangladesh.</Affiliation><Identifier Source="GRID">grid.412656.2</Identifier><Identifier Source="ISNI">0000 0004 0451 7306</Identifier></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Elsayed</LastName><ForeName>Khaled N M</ForeName><Initials>KNM</Initials><AffiliationInfo><Affiliation>Department of Botany, Faculty of Science, Beni-Suef University, Beni-Suef, Egypt.</Affiliation><Identifier Source="GRID">grid.411662.6</Identifier><Identifier Source="ISNI">0000 0004 0412 4932</Identifier></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahmed</LastName><ForeName>Sayed A</ForeName><Initials>SA</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</Affiliation><Identifier Source="GRID">grid.411662.6</Identifier><Identifier Source="ISNI">0000 0004 0412 4932</Identifier></AffiliationInfo></Author><Author ValidYN="Y"><LastName>El-Bassuony</LastName><ForeName>Ashraf A</ForeName><Initials>AA</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Faculty of Science, Beni-Suef University, Beni-Suef, 62511 Egypt.</Affiliation><Identifier Source="GRID">grid.411662.6</Identifier><Identifier Source="ISNI">0000 0004 0412 4932</Identifier></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mohamed</LastName><ForeName>Hussein S</ForeName><Initials>HS</Initials><AffiliationInfo><Affiliation>Research Institute of Medicinal and Aromatic Plants (RIMAP), Beni-Suef University, Beni-Suef City, Egypt.</Affiliation><Identifier Source="GRID">grid.411662.6</Identifier><Identifier Source="ISNI">0000 0004 0412 4932</Identifier></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2021</Year><Month>01</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Struct Chem</MedlineTA><NlmUniqueID>101582397</NlmUniqueID><ISSNLinking>1040-0400</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">COVID-19 virus protease</Keyword><Keyword MajorTopicYN="N">Caulerpin</Keyword><Keyword MajorTopicYN="N">MLSD</Keyword><Keyword MajorTopicYN="N">Molecular docking</Keyword><Keyword MajorTopicYN="N">Natural products</Keyword></KeywordList><CoiStatement>Conflict of interestThe authors declare that they have no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>06</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>12</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2021</Year><Month>1</Month><Day>13</Day><Hour>6</Hour><Minute>11</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2021</Year><Month>1</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2021</Year><Month>1</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33437137</ArticleId><ArticleId IdType="doi">10.1007/s11224-020-01723-5</ArticleId><ArticleId IdType="pii">1723</ArticleId><ArticleId IdType="pmc">PMC7791912</ArticleId></ArticleIdList><pmc-dir>pmcsd</pmc-dir>
<ReferenceList><Reference><Citation>Saudi Pharm J. 2018 Jul;26(5):685-693</Citation><ArticleIdList><ArticleId IdType="pubmed">29991912</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2012 Nov 14;134(45):18566-9</Citation><ArticleIdList><ArticleId IdType="pubmed">23106266</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 2018 Jul 2;46(W1):W329-W337</Citation><ArticleIdList><ArticleId IdType="pubmed">29860432</ArticleId></ArticleIdList></Reference><Reference><Citation>J Nat Prod. 2016 Mar 25;79(3):616-28</Citation><ArticleIdList><ArticleId IdType="pubmed">26900761</ArticleId></ArticleIdList></Reference><Reference><Citation>J Agric Food Chem. 2014 Jul 2;62(26):6130-7</Citation><ArticleIdList><ArticleId IdType="pubmed">24927286</ArticleId></ArticleIdList></Reference><Reference><Citation>Fish Shellfish Immunol. 2019 Dec;95:595-605</Citation><ArticleIdList><ArticleId IdType="pubmed">31676430</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Sci. 2018 Jan;27(1):331-340</Citation><ArticleIdList><ArticleId IdType="pubmed">29076577</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol Struct Dyn. 2020 Jun 24;:1-11</Citation><ArticleIdList><ArticleId IdType="pubmed">32579063</ArticleId></ArticleIdList></Reference><Reference><Citation>Phytother Res. 2017 Nov;31(11):1694-1701</Citation><ArticleIdList><ArticleId IdType="pubmed">28921681</ArticleId></ArticleIdList></Reference><Reference><Citation>Sci China Life Sci. 2020 Mar;63(3):457-460</Citation><ArticleIdList><ArticleId IdType="pubmed">32009228</ArticleId></ArticleIdList></Reference><Reference><Citation>Struct Chem. 2020 Jul 23;:1-22</Citation><ArticleIdList><ArticleId IdType="pubmed">32837118</ArticleId></ArticleIdList></Reference><Reference><Citation>J Med Invest. 2010 Aug;57(3-4):314-20</Citation><ArticleIdList><ArticleId IdType="pubmed">20847532</ArticleId></ArticleIdList></Reference><Reference><Citation>Comput Biol Chem. 2015 Dec;59 Pt A:81-6</Citation><ArticleIdList><ArticleId IdType="pubmed">26414950</ArticleId></ArticleIdList></Reference><Reference><Citation>Mar Drugs. 2014 Jun 18;12(6):3634-59</Citation><ArticleIdList><ArticleId IdType="pubmed">24945415</ArticleId></ArticleIdList></Reference><Reference><Citation>Medicines (Basel). 2016 Jan 28;3(1):</Citation><ArticleIdList><ArticleId IdType="pubmed">28930113</ArticleId></ArticleIdList></Reference><Reference><Citation>Drug Discov Today Technol. 2004 Dec;1(4):337-41</Citation><ArticleIdList><ArticleId IdType="pubmed">24981612</ArticleId></ArticleIdList></Reference><Reference><Citation>N Engl J Med. 2020 Feb 20;382(8):727-733</Citation><ArticleIdList><ArticleId IdType="pubmed">31978945</ArticleId></ArticleIdList></Reference><Reference><Citation>Pharm Biol. 2017 Dec;55(1):1239-1248</Citation><ArticleIdList><ArticleId IdType="pubmed">28262033</ArticleId></ArticleIdList></Reference><Reference><Citation>Interdiscip Sci. 2020 Sep;12(3):368-376</Citation><ArticleIdList><ArticleId IdType="pubmed">32488835</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS Comput Biol. 2009 May;5(5):e1000376</Citation><ArticleIdList><ArticleId IdType="pubmed">19412530</ArticleId></ArticleIdList></Reference><Reference><Citation>Antimicrob Agents Chemother. 1977 Oct;12(4):523-8</Citation><ArticleIdList><ArticleId IdType="pubmed">921248</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Trop. 2019 Mar;191:243-247</Citation><ArticleIdList><ArticleId IdType="pubmed">30659804</ArticleId></ArticleIdList></Reference><Reference><Citation>J Med Chem. 2006 Aug 24;49(17):5154-61</Citation><ArticleIdList><ArticleId IdType="pubmed">16913704</ArticleId></ArticleIdList></Reference><Reference><Citation>J Nat Prod. 2007 Aug;70(8):1360-3</Citation><ArticleIdList><ArticleId IdType="pubmed">17637068</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Cell. 2011 Apr;2(4):282-90</Citation><ArticleIdList><ArticleId IdType="pubmed">21533772</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2005 Apr 8;347(4):827-39</Citation><ArticleIdList><ArticleId IdType="pubmed">15769473</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11628-33</Citation><ArticleIdList><ArticleId IdType="pubmed">8876187</ArticleId></ArticleIdList></Reference><Reference><Citation>J Chem Inf Model. 2020 Jun 22;60(6):3277-3286</Citation><ArticleIdList><ArticleId IdType="pubmed">32315171</ArticleId></ArticleIdList></Reference><Reference><Citation>Springerplus. 2016 Jul 29;5(1):1210</Citation><ArticleIdList><ArticleId IdType="pubmed">27516948</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol Struct Dyn. 2020 Jun 11;:1-19</Citation><ArticleIdList><ArticleId IdType="pubmed">32462976</ArticleId></ArticleIdList></Reference><Reference><Citation>J Chem Inf Model. 2012 Nov 26;52(11):3099-105</Citation><ArticleIdList><ArticleId IdType="pubmed">23092397</ArticleId></ArticleIdList></Reference><Reference><Citation>Mini Rev Med Chem. 2019;19(9):751-761</Citation><ArticleIdList><ArticleId IdType="pubmed">28971770</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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