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2000
Volume 32, Issue 25
  • ISSN: 0929-8673
  • E-ISSN: 1875-533X

Abstract

Background

Pathogenic viruses that cause large-scale global or regional outbreaks almost always contain class I fusion proteins. Although the viruses differ in morphology, they all require fusion protein-mediated virus-host cell membranes during the early stages of host cell invasion.

Methods

The CHR region and NHR region of fusion proteins can form the 6-HB structure to drive the fusion pore formation between viruses and host cells through metastable interactions. Here, we obtained bifunctional N-peptides with inhibitory activities against two viruses, HIV-1 and MERS-CoV, based on the sequences in the HIV-1 NHR region by constructing N-trimer conformation interacting with the CHR region.

Results

This study demonstrates that N-peptides with the coiled triple helix structure obtained from the NHR region in 6-HB are able to target the CHR region and exhibit inhibitory activity against a variety of viruses.

Conclusion

Moreover, this strategy can be used to investigate antivirals against unknown viruses for future outbreaks.

© 2025 Bentham Science Publishers
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2025-09-07

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Structural Basis of HIV-1 gp41 N-trimer for Designing Bifunctional Peptide-based Fusion Inhibitors
Curr. Med. Chem. 32, 5321 (2025); https://doi.org/10.2174/0109298673291459240328074404
/content/journals/cmc/10.2174/0109298673291459240328074404
/content/journals/cmc/10.2174/0109298673291459240328074404
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  • Article Type:     Research Article
Keyword(s): bifunction; coiled triple helix structure; HIV-1; MERS-CoV; N-trimer; peptide-based fusion inhibitors

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