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2000
Volume 32, Issue 13
  • ISSN: 0929-8673
  • E-ISSN: 1875-533X

Abstract

SARS-CoV-2 has swept the world in recent years, triggering a global COVID-19 with a tremendous impact on human health and public safety. Similar to other coronaviruses, the six-helix bundle(6-HB) is not only a core structure driving the fusion of the SARS-CoV-2 envelope with the host cell membrane, but also the target of fusion inhibitors. The sequences from the HR1 or HR2 regions composing 6-HB are thus the original primary structures for the development of peptide-based fusion inhibitors. This review summarized the structure-activity relationship of the SARS-CoV-2 6-HB, analyzed the design methods and functional characteristics of peptide-based fusion inhibitors that contain different regions of HRs, and provided an outlook on the cutting-edge approaches for optimal modification of lead compounds (pan-coronavirization, chemical modification, superhelical construction, ). We hope that this review will provide researchers with a comprehensive understanding of the state-of-art research progress on both 6-HB and peptide-based fusion inhibitors of SARS-CoV-2, and provide some new insights for the development of antiviral drugs.

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/content/journals/cmc/10.2174/0109298673265694231113061842
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Structure and Function of the SARS-CoV-2 6-HB Fusion Core and Peptide-based Fusion Inhibitors: A Review
Curr. Med. Chem. 32, 2524 (2025); https://doi.org/10.2174/0109298673265694231113061842
/content/journals/cmc/10.2174/0109298673265694231113061842
/content/journals/cmc/10.2174/0109298673265694231113061842
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  • Article Type:     Review Article
Keyword(s): antiviral drugs; fusion inhibitors; hydrophobic residues; peptide; SARS-CoV-2; six-helix bundle

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