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Start Over Author "Chenchen Geng" Publisher american chemical society (acs)
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3. Stapled Peptides Targeting SARS-CoV-2 Spike Protein HR1 Inhibit the Fusion of Virus to Its Cell Receptor

Author

Si Chen, Chenchen Geng, Mengjun Zheng, Jie Qing, Wei-Dong Zhang, Yaxin Tang, Yan Zou, Huaxing Shen, Haoran Peng, Xiang Li, Honggang Hu, and Wei Cong

Subjects
chemistry.chemical_classification, Fusion, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Spike Protein, Lipid bilayer fusion, Acute respiratory disease, Peptide, Membrane Fusion, Virus, Cell biology, chemistry, Spike Glycoprotein, Coronavirus, Drug Discovery, Molecular Medicine, Receptor, Pandemics, Protein Binding
Abstract

The pandemic of acute respiratory disease in 2019 caused by highly pathogenic and infectious SARS-CoV-2 has seriously endangered human public safety. The 6-HB (HR1-HR2 complex) formation occurring in the process of spike protein-mediated membrane fusion could serve as a conserved and potential target for the design of fusion inhibitors. Based on the HR2 domain of 6-HB, we designed and synthesized 32 stapled peptides using an all-hydrocarbon peptide stapling strategy. Owing to the improved proteolytic stability and higher helical contents, the optimized stapled peptides termed SCH2-1-20 and SCH2-1-27 showed better inhibitory activities against pseudo and authentic SARS-CoV-2 compared to the linear counterpart. Of note, SCH2-1-20 and SCH2-1-27 were proved to interfere with S protein-mediated membrane fusion. Structural modeling indicated similar binding modes between SCH2-1-20 and the linear peptide. These optimized stapled peptides could serve as potent fusion inhibitors in treating and preventing SARS-CoV-2, and the corresponding SAR could facilitate further optimization.

Published
2021

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