ArticleAntimicrobial agents and chemotherapy2017
A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading.
Article in Antimicrobial agents and chemotherapy, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 51 citations in OpenAlex.
- Double-Stapled Peptide Scan Yields Potent Fusion Inhibitors of Respiratory Syncytial Virus.Journal of medicinal chemistry · 2026Article
- Structure-Guided Design of Peptide Inhibitors Targeting Class I Viral Fusion Proteins.Pathogens (Basel, Switzerland) · 2025Review
- Unleashing the Antiviral Potential of Stapled Peptides: A New Frontier in Combating Human Neurotropic Viral Infections.Microbial biotechnology · 2025Review
- Review
- Review
- AVP-GPT2: A Transformer-Powered Platform for De Novo Generation, Screening, and Explanation of Antiviral Peptides.Viruses · 2024Article
- Article
- Stapled peptides as potential inhibitors of SARS-CoV-2 binding to the hACE2 receptor.Journal of peptide science : an official publication of the European Peptide Society · 2022Review
- Leveraging the therapeutic, biological, and self-assembling potential of peptides for the treatment of viral infections.Journal of controlled release : official journal of the Controlled Release Society · 2022Review
- Review
- Depletion of TAX1BP1 Amplifies Innate Immune Responses during Respiratory Syncytial Virus Infection.Journal of virology · 2021Article
- Human Coronaviruses: Counteracting the Damage by Storm.Viruses · 2021Review
- Review
- Article
- Antimicrobial peptides - Advances in development of therapeutic applications.Life sciences · 2020Review
- Targeting the Respiratory Syncytial Virus NAntimicrobial agents and chemotherapy · 2020Article
- Macrocyclization of an all-d linear α-helical peptide imparts cellular permeability.Chemical science · 2020Article
- Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.Peptide science (Hoboken, N.J.) · 2020Article
- Coronavirus envelope protein: current knowledge.Virology journal · 2019Review
- Biochemical characterization of the respiratory syncytial virus NThe Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synthetic peptides derived from the heptad repeat (HR) of fusion (F) proteins can be used as dominant negative inhibitors to inhibit the fusion mechanism of class I viral F proteins. Here, we have performed a stapled-peptide scan across the HR2 domain of the respiratory syncytial virus (RSV) F protein with the aim to identify a minimal domain capable of disrupting the formation of the postfusion six-helix bundle required for viral cell entry. Constraining the peptides with a single staple was not sufficient to inhibit RSV infection. However, the insertion of double staples led to the identification of novel short stapled peptides that display nanomolar potency in HEp-2 cells and are exceptionally robust to proteolytic degradation. By replacing each amino acid of the peptides by an alanine, we found that the substitution of residues 506 to 509, located in a patch of polar contacts between HR2 and HR1, severely affected inhibition. Finally, we show that intranasal delivery of the most potent peptide to BALB/c mice significantly decreased RSV infection in upper and lower respiratory tracts. The discovery of this minimal HR2 sequence as a means for inhibition of RSV infection provides the basis for further medicinal chemistry efforts toward developing RSV fusion antivirals.
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Registered trials
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.