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De Novo Design of alpha-Helical Lipopeptides Targeting Viral Fusion Proteins: A Promising Strategy for Relatively Broad-Spectrum Antiviral Drug Discovery
First author：Wang Chao,Zhao Lei,Xia Shuai,Zhang Tianhong
Corresponding author：Zhong Wu,Jiang Shibo,Liu Keliang
essential_information
- Person in charge：Wang Chao,Zhao Lei,Xia Shuai,Zhang Tianhong
- Data Sources： OTHERS
- Number of papers：OTHERS20190615
- Published time：2018-09-07
2018-09-07
Published articles
Journal：J. Med. Chem.
Publication type: Research Article
IF(IF): 6.054
PMID: 30192544 Link To Pubmed Full text Download
Background And Purpose
Method
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).
Conclusion
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 multi-helix motif.