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/Corpus ); 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 ; Lei Zhao ; Shuai Xia ; Tianhong Zhang ; Ruiyuan Cao ; Guodong Liang ; Yue Li ; Guangpeng Meng ; Weicong Wang ; Weiguo Shi ; Wu Zhong ; Shibo Jiang ; Keliang LiuSource :
- Journal of medicinal chemistry [ 1520-4804 ] ; 2018.
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
Links to Exploration step
pubmed:30192544Le document en format XML
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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>
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<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>
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