Evidence map›Paper›PMID 38584558›Full record

ArticleCurrent medicinal chemistry2025

Structural Basis of HIV-1 gp41 N-trimer for Designing Bifunctional Peptide-based Fusion Inhibitors.

Jinlin Wang, Peiying Li, Ruijuan Li, Guodong Liang, Yuheng Ma, Heiya Na

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Article in Current medicinal chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

6 authors.

Jinlin WangKey Laboratory for Candidate Drug Design and Screening Based on Chemical Biology, College of Pharmacy, Inner Mongolia Medical University, Hohhot, P.R. China.
Peiying LiDepartment of Pediatrics, Fifth Medical Centre of Chinese PLA General Hospital, Beijing, P.R. China.
Ruijuan LiKey Laboratory for Candidate Drug Design and Screening Based on Chemical Biology, College of Pharmacy, Inner Mongolia Medical University, Hohhot, P.R. China.
Guodong LiangKey Laboratory for Candidate Drug Design and Screening Based on Chemical Biology, College of Pharmacy, Inner Mongolia Medical University, Hohhot, P.R. China.ORCID 0009-0008-6278-0379
Yuheng MaKey Laboratory for Candidate Drug Design and Screening Based on Chemical Biology, College of Pharmacy, Inner Mongolia Medical University, Hohhot, P.R. China.
Heiya NaCollege of Life Sciences, Inner Mongolia Agricultural University, Hohhot, P.R. China.

Funding

Inner Mongolia Medical University Talent Program of China ZY0120016Inner Mongolia Medical University Youth Project of China YKD2023QN053Inner Mongolia Natural Science Foundation of China 2023LHMS08045National Natural Science Foundation of China 82060624
6 · The paper itself

Abstract

backgroundPathogenic 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.

methodsThe 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.

resultsThis 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.

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

Indexed as

Antiviral AgentsDrug DesignHIV-1HIV Envelope Protein gp41HIV Fusion InhibitorsPeptidesAmino Acid SequenceHumansStructure-Activity RelationshipAntiviral Agentsgp41 protein, Human immunodeficiency virus 1HIV Envelope Protein gp41HIV Fusion InhibitorsPeptidesbifunctioncoiled triple helix structure.HIV-1MERS-CoVN-trimerpeptide-based fusion inhibitors

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.