Binding interaction of quercetin-3-beta-galactoside and its synthetic derivatives with SARS-CoV 3CL(pro): structure-activity relationship studies reveal salient pharmacophore features.
Identifieur interne : 002276 ( PubMed/Checkpoint ); précédent : 002275; suivant : 002277Binding interaction of quercetin-3-beta-galactoside and its synthetic derivatives with SARS-CoV 3CL(pro): structure-activity relationship studies reveal salient pharmacophore features.
Auteurs : Lili Chen [République populaire de Chine] ; Jian Li ; Cheng Luo ; Hong Liu ; Weijun Xu ; Gang Chen ; Oi Wah Liew ; Weiliang Zhu ; Chum Mok Puah ; Xu Shen ; Hualiang JiangSource :
- Bioorganic & medicinal chemistry [ 0968-0896 ] ; 2006.
Descripteurs français
- KwdFr :
- Conception de médicament, Cysteine endopeptidases (), Cysteine endopeptidases (génétique), Cysteine endopeptidases (métabolisme), Humains, Inhibiteurs de protéases (pharmacologie), Modèles moléculaires, Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Quercétine (), Quercétine (analogues et dérivés), Quercétine (pharmacologie), Quercétine (synthèse chimique), Relation structure-activité, Sites de fixation, Structure moléculaire, Virus du SRAS (enzymologie).
- MESH :
- analogues et dérivés : Quercétine.
- enzymologie : Virus du SRAS.
- génétique : Cysteine endopeptidases, Protéines virales.
- métabolisme : Cysteine endopeptidases, Protéines virales.
- pharmacologie : Inhibiteurs de protéases, Quercétine.
- synthèse chimique : Quercétine.
- Conception de médicament, Cysteine endopeptidases, Humains, Modèles moléculaires, Protéines virales, Quercétine, Relation structure-activité, Sites de fixation, Structure moléculaire.
English descriptors
- KwdEn :
- Binding Sites, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Drug Design, Humans, Models, Molecular, Molecular Structure, Protease Inhibitors (pharmacology), Quercetin (analogs & derivatives), Quercetin (chemical synthesis), Quercetin (chemistry), Quercetin (pharmacology), SARS Virus (enzymology), Structure-Activity Relationship, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , analogs & derivatives : Quercetin.
- chemical , chemical synthesis : Quercetin.
- chemical , chemistry : Cysteine Endopeptidases, Quercetin, Viral Proteins.
- chemical , genetics : Cysteine Endopeptidases, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- chemical , pharmacology : Protease Inhibitors, Quercetin.
- enzymology : SARS Virus.
- Binding Sites, Drug Design, Humans, Models, Molecular, Molecular Structure, Structure-Activity Relationship.
Abstract
The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is one of the most promising targets for discovery of drugs against SARS, because of its critical role in the viral life cycle. In this study, a natural compound called quercetin-3-beta-galactoside was identified as an inhibitor of the protease by molecular docking, SPR/FRET-based bioassays, and mutagenesis studies. Both molecular modeling and Q189A mutation revealed that Gln189 plays a key role in the binding. Furthermore, experimental evidence showed that the secondary structure and enzymatic activity of SARS-CoV 3CL(pro) were not affected by the Q189A mutation. With the help of molecular modeling, eight new derivatives of the natural product were designed and synthesized. Bioassay results reveal salient features of the structure-activity relationship of the new compounds: (1) removal of the 7-hydroxy group of the quercetin moiety decreases the bioactivity of the derivatives; (2) acetoxylation of the sugar moiety abolishes inhibitor action; (3) introduction of a large sugar substituent on 7-hydroxy of quercetin can be tolerated; (4) replacement of the galactose moiety with other sugars does not affect inhibitor potency. This study not only reveals a new class of compounds as potential drug leads against the SARS virus, but also provides a solid understanding of the mechanism of inhibition against the target enzyme.
DOI: 10.1016/j.bmc.2006.09.014
PubMed: 17046271
Affiliations:
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uniqKey="Xu W" first="Weijun" last="Xu">Weijun Xu</name></author><author><name sortKey="Chen, Gang" sort="Chen, Gang" uniqKey="Chen G" first="Gang" last="Chen">Gang Chen</name></author><author><name sortKey="Liew, Oi Wah" sort="Liew, Oi Wah" uniqKey="Liew O" first="Oi Wah" last="Liew">Oi Wah Liew</name></author><author><name sortKey="Zhu, Weiliang" sort="Zhu, Weiliang" uniqKey="Zhu W" first="Weiliang" last="Zhu">Weiliang Zhu</name></author><author><name sortKey="Puah, Chum Mok" sort="Puah, Chum Mok" uniqKey="Puah C" first="Chum Mok" last="Puah">Chum Mok Puah</name></author><author><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name></author><author><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name></author></analytic><series><title level="j">Bioorganic & medicinal chemistry</title><idno type="ISSN">0968-0896</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Cysteine Endopeptidases (chemistry)</term><term>Cysteine Endopeptidases (genetics)</term><term>Cysteine Endopeptidases (metabolism)</term><term>Drug Design</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Structure</term><term>Protease Inhibitors (pharmacology)</term><term>Quercetin (analogs & derivatives)</term><term>Quercetin (chemical synthesis)</term><term>Quercetin (chemistry)</term><term>Quercetin (pharmacology)</term><term>SARS Virus (enzymology)</term><term>Structure-Activity Relationship</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conception de médicament</term><term>Cysteine endopeptidases ()</term><term>Cysteine endopeptidases (génétique)</term><term>Cysteine endopeptidases (métabolisme)</term><term>Humains</term><term>Inhibiteurs de protéases (pharmacologie)</term><term>Modèles moléculaires</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Protéines virales (métabolisme)</term><term>Quercétine ()</term><term>Quercétine (analogues et dérivés)</term><term>Quercétine (pharmacologie)</term><term>Quercétine (synthèse chimique)</term><term>Relation structure-activité</term><term>Sites de fixation</term><term>Structure moléculaire</term><term>Virus du SRAS (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Quercetin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Quercetin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Quercetin</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protease Inhibitors</term><term>Quercetin</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Quercétine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de protéases</term><term>Quercétine</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Quercétine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Drug Design</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Structure</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conception de médicament</term><term>Cysteine endopeptidases</term><term>Humains</term><term>Modèles moléculaires</term><term>Protéines virales</term><term>Quercétine</term><term>Relation structure-activité</term><term>Sites de fixation</term><term>Structure moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is one of the most promising targets for discovery of drugs against SARS, because of its critical role in the viral life cycle. In this study, a natural compound called quercetin-3-beta-galactoside was identified as an inhibitor of the protease by molecular docking, SPR/FRET-based bioassays, and mutagenesis studies. Both molecular modeling and Q189A mutation revealed that Gln189 plays a key role in the binding. Furthermore, experimental evidence showed that the secondary structure and enzymatic activity of SARS-CoV 3CL(pro) were not affected by the Q189A mutation. With the help of molecular modeling, eight new derivatives of the natural product were designed and synthesized. Bioassay results reveal salient features of the structure-activity relationship of the new compounds: (1) removal of the 7-hydroxy group of the quercetin moiety decreases the bioactivity of the derivatives; (2) acetoxylation of the sugar moiety abolishes inhibitor action; (3) introduction of a large sugar substituent on 7-hydroxy of quercetin can be tolerated; (4) replacement of the galactose moiety with other sugars does not affect inhibitor potency. This study not only reveals a new class of compounds as potential drug leads against the SARS virus, but also provides a solid understanding of the mechanism of inhibition against the target enzyme.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17046271</PMID><DateCompleted><Year>2007</Year><Month>02</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0968-0896</ISSN><JournalIssue CitedMedium="Print"><Volume>14</Volume><Issue>24</Issue><PubDate><Year>2006</Year><Month>Dec</Month><Day>15</Day></PubDate></JournalIssue><Title>Bioorganic & medicinal chemistry</Title><ISOAbbreviation>Bioorg. Med. Chem.</ISOAbbreviation></Journal><ArticleTitle>Binding interaction of quercetin-3-beta-galactoside and its synthetic derivatives with SARS-CoV 3CL(pro): structure-activity relationship studies reveal salient pharmacophore features.</ArticleTitle><Pagination><MedlinePgn>8295-306</MedlinePgn></Pagination><Abstract><AbstractText>The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is one of the most promising targets for discovery of drugs against SARS, because of its critical role in the viral life cycle. In this study, a natural compound called quercetin-3-beta-galactoside was identified as an inhibitor of the protease by molecular docking, SPR/FRET-based bioassays, and mutagenesis studies. Both molecular modeling and Q189A mutation revealed that Gln189 plays a key role in the binding. Furthermore, experimental evidence showed that the secondary structure and enzymatic activity of SARS-CoV 3CL(pro) were not affected by the Q189A mutation. With the help of molecular modeling, eight new derivatives of the natural product were designed and synthesized. Bioassay results reveal salient features of the structure-activity relationship of the new compounds: (1) removal of the 7-hydroxy group of the quercetin moiety decreases the bioactivity of the derivatives; (2) acetoxylation of the sugar moiety abolishes inhibitor action; (3) introduction of a large sugar substituent on 7-hydroxy of quercetin can be tolerated; (4) replacement of the galactose moiety with other sugars does not affect inhibitor potency. This study not only reveals a new class of compounds as potential drug leads against the SARS virus, but also provides a solid understanding of the mechanism of inhibition against the target enzyme.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Lili</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Jian</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Cheng</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Hong</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Weijun</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Gang</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Liew</LastName><ForeName>Oi Wah</ForeName><Initials>OW</Initials></Author><Author ValidYN="Y"><LastName>Zhu</LastName><ForeName>Weiliang</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Puah</LastName><ForeName>Chum Mok</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Xu</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Hualiang</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>10</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Bioorg Med Chem</MedlineTA><NlmUniqueID>9413298</NlmUniqueID><ISSNLinking>0968-0896</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>8O1CR18L82</RegistryNumber><NameOfSubstance UI="C021304">hyperoside</NameOfSubstance></Chemical><Chemical><RegistryNumber>9IKM0I5T1E</RegistryNumber><NameOfSubstance UI="D011794">Quercetin</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="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015195" MajorTopicYN="N">Drug Design</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011794" MajorTopicYN="N">Quercetin</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">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="Q000737" 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IdType="pubmed">11394736</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Chen, Gang" sort="Chen, Gang" uniqKey="Chen G" first="Gang" last="Chen">Gang Chen</name><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name><name sortKey="Li, Jian" sort="Li, Jian" uniqKey="Li J" first="Jian" last="Li">Jian Li</name><name sortKey="Liew, Oi Wah" sort="Liew, Oi Wah" uniqKey="Liew O" first="Oi Wah" last="Liew">Oi Wah Liew</name><name sortKey="Liu, Hong" sort="Liu, Hong" uniqKey="Liu H" first="Hong" last="Liu">Hong Liu</name><name sortKey="Luo, Cheng" sort="Luo, Cheng" uniqKey="Luo C" first="Cheng" last="Luo">Cheng Luo</name><name sortKey="Puah, Chum Mok" sort="Puah, Chum Mok" uniqKey="Puah C" first="Chum Mok" last="Puah">Chum Mok Puah</name><name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name><name sortKey="Xu, Weijun" sort="Xu, Weijun" uniqKey="Xu W" first="Weijun" last="Xu">Weijun Xu</name><name sortKey="Zhu, Weiliang" sort="Zhu, Weiliang" uniqKey="Zhu W" first="Weiliang" last="Zhu">Weiliang Zhu</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Chen, Lili" sort="Chen, Lili" uniqKey="Chen L" first="Lili" last="Chen">Lili Chen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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