De Novo Design of α-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery
Identifieur interne : 001F55 ( Ncbi/Curation ); précédent : 001F54; suivant : 001F56De 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, États-Unis] ; Keliang Liu [République populaire de Chine]Source :
- Journal of Medicinal Chemistry [ 0022-2623 ] ; 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.
Url:
DOI: 10.1021/acs.jmedchem.8b00890
PubMed: 30192544
PubMed Central: 7075651
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PMC:7075651Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">De Novo Design
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Targeting Viral Fusion Proteins: A Promising Strategy for Relatively
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Cao, Ruiyuan" sort="Cao, Ruiyuan" uniqKey="Cao R" first="Ruiyuan" last="Cao">Ruiyuan Cao</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">State Key Laboratory of Toxicology and Medical Countermeasures,<institution>Beijing Institute of Pharmacology and Toxicology</institution>
, 27 Tai-Ping Road, Beijing 100850,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Liang, Guodong" sort="Liang, Guodong" uniqKey="Liang G" first="Guodong" last="Liang">Guodong Liang</name>
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, 27 Tai-Ping Road, Beijing 100850,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
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<author><name sortKey="Li, Yue" sort="Li, Yue" uniqKey="Li Y" first="Yue" last="Li">Yue Li</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Key Laboratory of Structure-Based Drug Design & Discovery of the Ministry of Education,<institution>Shenyang Pharmaceutical University</institution>
, Shenyang 110016,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
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<author><name sortKey="Meng, Guangpeng" sort="Meng, Guangpeng" uniqKey="Meng G" first="Guangpeng" last="Meng">Guangpeng Meng</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Key Laboratory of Structure-Based Drug Design & Discovery of the Ministry of Education,<institution>Shenyang Pharmaceutical University</institution>
, Shenyang 110016,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Wang, Weicong" sort="Wang, Weicong" uniqKey="Wang W" first="Weicong" last="Wang">Weicong Wang</name>
<affiliation wicri:level="1"><nlm:aff id="aff5">Department of Clinical Trial Center, China National Clinical Research Center for Neurological Diseases, Beijing Tiantan Hospital,<institution>Capital Medical University</institution>
, Beijing 100050,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Shi, Weiguo" sort="Shi, Weiguo" uniqKey="Shi W" first="Weiguo" last="Shi">Weiguo Shi</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">State Key Laboratory of Toxicology and Medical Countermeasures,<institution>Beijing Institute of Pharmacology and Toxicology</institution>
, 27 Tai-Ping Road, Beijing 100850,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Zhong, Wu" sort="Zhong, Wu" uniqKey="Zhong W" first="Wu" last="Zhong">Wu Zhong</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">State Key Laboratory of Toxicology and Medical Countermeasures,<institution>Beijing Institute of Pharmacology and Toxicology</institution>
, 27 Tai-Ping Road, Beijing 100850,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name>
<affiliation wicri:level="1"><nlm:aff id="aff2">Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences & Shanghai Public Health Clinical Center,<institution>Fudan University</institution>
, 130 Dong An Road, Shanghai 200032,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff4">Lindsley F. Kimball Research Institute,<institution>New York Blood Center</institution>
, New York, New York 10065,<country>United States</country>
;</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<affiliation wicri:level="1"><nlm:aff id="aff1">State Key Laboratory of Toxicology and Medical Countermeasures,<institution>Beijing Institute of Pharmacology and Toxicology</institution>
, 27 Tai-Ping Road, Beijing 100850,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Antiviral Agents (chemistry)</term>
<term>Antiviral Agents (pharmacology)</term>
<term>Coronavirus Infections (drug therapy)</term>
<term>Coronavirus Infections (virology)</term>
<term>Drug Discovery</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Influenza, Human (drug therapy)</term>
<term>Influenza, Human (virology)</term>
<term>Influenzavirus A (drug effects)</term>
<term>Lipopeptides (chemistry)</term>
<term>Lipopeptides (pharmacology)</term>
<term>Middle East Respiratory Syndrome Coronavirus (drug effects)</term>
<term>Protein Conformation, alpha-Helical</term>
<term>Viral Fusion Proteins (antagonists & inhibitors)</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux ()</term>
<term>Antiviraux (pharmacologie)</term>
<term>Cellules HEK293</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient ()</term>
<term>Découverte de médicament</term>
<term>Grippe humaine (traitement médicamenteux)</term>
<term>Grippe humaine (virologie)</term>
<term>Humains</term>
<term>Infections à coronavirus (traitement médicamenteux)</term>
<term>Infections à coronavirus (virologie)</term>
<term>Influenzavirus A ()</term>
<term>Lipopeptides ()</term>
<term>Lipopeptides (pharmacologie)</term>
<term>Protéines de fusion virale (antagonistes et inhibiteurs)</term>
<term>Pénétration virale</term>
<term>Structure en hélice alpha</term>
<term>Séquence d'acides aminés</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Viral Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term>
<term>Lipopeptides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term>
<term>Lipopeptides</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protéines de fusion virale</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Influenzavirus A</term>
<term>Middle East Respiratory Syndrome Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Coronavirus Infections</term>
<term>Influenza, Human</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term>
<term>Lipopeptides</term>
</keywords>
<keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Grippe humaine</term>
<term>Infections à coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe humaine</term>
<term>Infections à coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term>
<term>Influenza, Human</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Drug Discovery</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Protein Conformation, alpha-Helical</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Antiviraux</term>
<term>Cellules HEK293</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient</term>
<term>Découverte de médicament</term>
<term>Humains</term>
<term>Influenzavirus A</term>
<term>Lipopeptides</term>
<term>Pénétration virale</term>
<term>Structure en hélice alpha</term>
<term>Séquence d'acides aminés</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p content-type="toc-graphic"><graphic xlink:href="jm8b00890_0008" id="ab-tgr1"></graphic>
</p>
<p>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.</p>
</div>
</front>
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