De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.
Identifieur interne : 000789 ( PubMed/Curation ); précédent : 000788; suivant : 000790De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.
Auteurs : Chao Wang [République populaire de Chine] ; Lei Zhao [République populaire de Chine] ; Shuai Xia [République populaire de Chine] ; Tianhong Zhang [République populaire de Chine] ; Ruiyuan Cao [République populaire de Chine] ; Guodong Liang [République populaire de Chine] ; Yue Li [République populaire de Chine] ; Guangpeng Meng [République populaire de Chine] ; Weicong Wang [République populaire de Chine] ; Weiguo Shi [République populaire de Chine] ; Wu Zhong [République populaire de Chine] ; Shibo Jiang [République populaire de Chine] ; Keliang Liu [République populaire de Chine]Source :
- Journal of medicinal chemistry [ 1520-4804 ] ; 2018.
Descripteurs français
- KwdFr :
- Antiviraux (), Antiviraux (pharmacologie), Cellules HEK293, Coronavirus du syndrome respiratoire du Moyen-Orient (), Découverte de médicament, Grippe humaine (traitement médicamenteux), Grippe humaine (virologie), Humains, Infections à coronavirus (traitement médicamenteux), Infections à coronavirus (virologie), Influenzavirus A (), Lipopeptides (), Lipopeptides (pharmacologie), Protéines de fusion virale (antagonistes et inhibiteurs), Pénétration virale, Structure en hélice alpha, Séquence d'acides aminés.
- MESH :
- antagonistes et inhibiteurs : Protéines de fusion virale.
- pharmacologie : Antiviraux, Lipopeptides.
- traitement médicamenteux : Grippe humaine, Infections à coronavirus.
- virologie : Grippe humaine, Infections à coronavirus.
- Antiviraux, Cellules HEK293, Coronavirus du syndrome respiratoire du Moyen-Orient, Découverte de médicament, Humains, Influenzavirus A, Lipopeptides, Pénétration virale, Structure en hélice alpha, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Coronavirus Infections (drug therapy), Coronavirus Infections (virology), Drug Discovery, HEK293 Cells, Humans, Influenza, Human (drug therapy), Influenza, Human (virology), Influenzavirus A (drug effects), Lipopeptides (chemistry), Lipopeptides (pharmacology), Middle East Respiratory Syndrome Coronavirus (drug effects), Protein Conformation, alpha-Helical, Viral Fusion Proteins (antagonists & inhibitors), Virus Internalization.
- MESH :
- chemical , antagonists & inhibitors : Viral Fusion Proteins.
- chemical , chemistry : Antiviral Agents, Lipopeptides.
- chemical , pharmacology : Antiviral Agents, Lipopeptides.
- drug effects : Influenzavirus A, Middle East Respiratory Syndrome Coronavirus.
- drug therapy : Coronavirus Infections, Influenza, Human.
- virology : Coronavirus Infections, Influenza, Human.
- Amino Acid Sequence, Drug Discovery, HEK293 Cells, Humans, Protein Conformation, alpha-Helical, Virus Internalization.
Abstract
Class I enveloped viruses share similarities in their apparent use of a hexameric coiled-coil assembly to drive the merging of virus and host cell membranes. Inhibition of coiled coil-mediated interactions using bioactive peptides that replicate an α-helical chain from the viral fusion machinery has significant antiviral potential. Here, we present the construction of a series of lipopeptides composed of a de novo heptad repeat sequence-based α-helical peptide plus a hydrocarbon tail. Promisingly, the constructs adopted stable α-helical conformations and exhibited relatively broad-spectrum antiviral activities against Middle East respiratory syndrome coronavirus (MERS-CoV) and influenza A viruses (IAVs). Together, these findings reveal a new strategy for relatively broad-spectrum antiviral drug discovery by relying on the tunability of the α-helical coiled-coil domains present in all class I fusion proteins and the amphiphilic nature of the individual helices from this multihelix motif.
DOI: 10.1021/acs.jmedchem.8b00890
PubMed: 30192544
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<front><div type="abstract" xml:lang="en">Class I enveloped viruses share similarities in their apparent use of a hexameric coiled-coil assembly to drive the merging of virus and host cell membranes. Inhibition of coiled coil-mediated interactions using bioactive peptides that replicate an α-helical chain from the viral fusion machinery has significant antiviral potential. Here, we present the construction of a series of lipopeptides composed of a de novo heptad repeat sequence-based α-helical peptide plus a hydrocarbon tail. Promisingly, the constructs adopted stable α-helical conformations and exhibited relatively broad-spectrum antiviral activities against Middle East respiratory syndrome coronavirus (MERS-CoV) and influenza A viruses (IAVs). Together, these findings reveal a new strategy for relatively broad-spectrum antiviral drug discovery by relying on the tunability of the α-helical coiled-coil domains present in all class I fusion proteins and the amphiphilic nature of the individual helices from this multihelix motif.</div>
</front>
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<Month>10</Month>
<Day>07</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4804</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>61</Volume>
<Issue>19</Issue>
<PubDate><Year>2018</Year>
<Month>10</Month>
<Day>11</Day>
</PubDate>
</JournalIssue>
<Title>Journal of medicinal chemistry</Title>
<ISOAbbreviation>J. Med. Chem.</ISOAbbreviation>
</Journal>
<ArticleTitle>De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery.</ArticleTitle>
<Pagination><MedlinePgn>8734-8745</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.jmedchem.8b00890</ELocationID>
<Abstract><AbstractText>Class I enveloped viruses share similarities in their apparent use of a hexameric coiled-coil assembly to drive the merging of virus and host cell membranes. Inhibition of coiled coil-mediated interactions using bioactive peptides that replicate an α-helical chain from the viral fusion machinery has significant antiviral potential. Here, we present the construction of a series of lipopeptides composed of a de novo heptad repeat sequence-based α-helical peptide plus a hydrocarbon tail. Promisingly, the constructs adopted stable α-helical conformations and exhibited relatively broad-spectrum antiviral activities against Middle East respiratory syndrome coronavirus (MERS-CoV) and influenza A viruses (IAVs). Together, these findings reveal a new strategy for relatively broad-spectrum antiviral drug discovery by relying on the tunability of the α-helical coiled-coil domains present in all class I fusion proteins and the amphiphilic nature of the individual helices from this multihelix motif.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Chao</ForeName>
<Initials>C</Initials>
<Identifier Source="ORCID">0000-0002-7673-0638</Identifier>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhao</LastName>
<ForeName>Lei</ForeName>
<Initials>L</Initials>
<Identifier Source="ORCID">0000-0003-2952-1187</Identifier>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xia</LastName>
<ForeName>Shuai</ForeName>
<Initials>S</Initials>
<Identifier Source="ORCID">0000-0002-1390-5533</Identifier>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences & Shanghai Public Health Clinical Center , Fudan University , 130 Dong An Road , Shanghai 200032 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Tianhong</ForeName>
<Initials>T</Initials>
<Identifier Source="ORCID">0000-0002-9798-2324</Identifier>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cao</LastName>
<ForeName>Ruiyuan</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liang</LastName>
<ForeName>Guodong</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Yue</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Structure-Based Drug Design & Discovery of the Ministry of Education , Shenyang Pharmaceutical University , Shenyang 110016 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Meng</LastName>
<ForeName>Guangpeng</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Structure-Based Drug Design & Discovery of the Ministry of Education , Shenyang Pharmaceutical University , Shenyang 110016 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Weicong</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Department of Clinical Trial Center, China National Clinical Research Center for Neurological Diseases, Beijing Tiantan Hospital , Capital Medical University , Beijing 100050 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Weiguo</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhong</LastName>
<ForeName>Wu</ForeName>
<Initials>W</Initials>
<Identifier Source="ORCID">0000-0002-0536-620X</Identifier>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jiang</LastName>
<ForeName>Shibo</ForeName>
<Initials>S</Initials>
<Identifier Source="ORCID">0000-0003-1493-6523</Identifier>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences & Shanghai Public Health Clinical Center , Fudan University , 130 Dong An Road , Shanghai 200032 , China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute , New York Blood Center , New York , New York 10065 , United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Keliang</ForeName>
<Initials>K</Initials>
<Identifier Source="ORCID">0000-0002-9133-377X</Identifier>
<AffiliationInfo><Affiliation>State Key Laboratory of Toxicology and Medical Countermeasures , Beijing Institute of Pharmacology and Toxicology , 27 Tai-Ping Road , Beijing 100850 , China.</Affiliation>
</AffiliationInfo>
</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>2018</Year>
<Month>09</Month>
<Day>19</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Med Chem</MedlineTA>
<NlmUniqueID>9716531</NlmUniqueID>
<ISSNLinking>0022-2623</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D055666">Lipopeptides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014760">Viral Fusion Proteins</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="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName>
<QualifierName UI="Q000188" MajorTopicYN="Y">drug therapy</QualifierName>
<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055808" MajorTopicYN="Y">Drug Discovery</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007251" MajorTopicYN="N">Influenza, Human</DescriptorName>
<QualifierName UI="Q000188" MajorTopicYN="Y">drug therapy</QualifierName>
<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029521" MajorTopicYN="N">Influenzavirus A</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
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<MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D000072756" MajorTopicYN="N">Protein Conformation, alpha-Helical</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014760" MajorTopicYN="N">Viral Fusion Proteins</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053586" MajorTopicYN="N">Virus Internalization</DescriptorName>
</MeshHeading>
</MeshHeadingList>
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<Day>8</Day>
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