ArticleJournal of virology2020
Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers.
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Who cites it
161 citing papers in PubMed, 223 citations in OpenAlex.
- The efficacy and safety of inhaled peptide YKYY017 for COVID-19 patients with mild illness: a phase 2 randomized controlled trial.Nature communications · 2025Trial
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- ACE2- and HR2-Mimetic Peptides Inhibit Replication of Two SARS-CoV-2 Variants.Journal of medical virology · 2026Article
- CGM23 corresponds to a pan-coronavirus lipopeptide inhibitor potently inhibiting virion fusion.iScience · 2026Article
- Molecular basis of fox ACE2 recognition by receptor binding domains of SARS-CoV-2 and PCoV-GD.Cell insight · 2026Article
- Structure-Guided Design of Peptide Inhibitors Targeting Class I Viral Fusion Proteins.Pathogens (Basel, Switzerland) · 2025Review
- The Role of ACE2 in SARS-CoV-2 Infection, Pathogenesis, and Antiviral Interventions.Journal of medical virology · 2025Review
- A novel linear B-cell epitope on S2 protein of transmissible gastroenteritis virus identified using a monoclonal antibody.BMC veterinary research · 2025Article
- Membrane-Targeting Antivirals.International journal of molecular sciences · 2025Review
- Membrane-wide screening identifies potential tissue-specific determinants of SARS-CoV-2 tropism.PLoS pathogens · 2025Article
- A Dual-Targeting Peptide Inhibitor Simultaneously Blocking Viral Attachment and Membrane Fusion for Broad-Spectrum Inhibition of SARS-CoV-2.International journal of molecular sciences · 2025Article
- Capture of fusion-intermediate conformations of SARS-CoV-2 spike requires receptor binding and cleavage at either the S1/S2 or S2' site.PLoS pathogens · 2025Article
- Enhancing the solubility of SARS-CoV-2 inhibitors to increase future prospects for clinical development.Journal of virology · 2025Article
- Development of Receptor-Integrated Magnetically Labeled Liposomes for Investigating SARS-CoV-2 Fusion Interactions.Analytical chemistry · 2025Article
- Article
- Computational optimization of a pan-coronavirus fusion inhibitory peptide targeting spike's heptapeptide repeat region.Biosafety and health · 2025Article
- Advancements in Structural Basis of Covalent Inhibitors Targeting SARS-CoV-2 Essential Proteins.Current medicinal chemistry · 2025Review
- Structure and Function of the SARS-CoV-2 6-HB Fusion Core and Peptide-based Fusion Inhibitors: A Review.Current medicinal chemistry · 2025Review
- DiMA: sequence diversity dynamics analyser for viruses.Briefings in bioinformatics · 2024Article
- Article
101 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 2019 coronavirus disease (COVID-19), caused by the emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has posed serious threats to global public health and economic and social stabilities, calling for the prompt development of therapeutics and prophylactics. In this study, we first verified that SARS-CoV-2 uses human angiotensin-converting enzyme 2 (ACE2) as a cell receptor and that its spike (S) protein mediates high membrane fusion activity. The heptad repeat 1 (HR1) sequence in the S2 fusion protein of SARS-CoV-2 possesses markedly increased α-helicity and thermostability, as well as a higher binding affinity with its corresponding heptad repeat 2 (HR2) site, than the HR1 sequence in S2 of severe acute respiratory syndrome coronavirus (SARS-CoV). Then, we designed an HR2 sequence-based lipopeptide fusion inhibitor, termed IPB02, which showed highly potent activities in inhibiting SARS-CoV-2 S protein-mediated cell-cell fusion and pseudovirus transduction. IPB02 also inhibited the SARS-CoV pseudovirus efficiently. Moreover, the structure-activity relationship (SAR) of IPB02 was characterized with a panel of truncated lipopeptides, revealing the amino acid motifs critical for its binding and antiviral capacities. Therefore, the results presented here provide important information for understanding the entry pathway of SARS-CoV-2 and the design of antivirals that target the membrane fusion step.
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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.