ArticleJournal of the American Chemical Society2005
Inhibiting HIV fusion with a beta-peptide foldamer.
Article in Journal of the American Chemical Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
51 citing papers in PubMed, 173 citations in OpenAlex.
- From Concepts to Inhibitors: A Blueprint for Targeting Protein-Protein Interactions.Chemical reviews · 2025Review
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Peptide foldamer-based inhibitors of the SARS-CoV-2 S protein-human ACE2 interaction.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Design and Evaluation of Ambiphilic Aryl Thiol-Iminium-Based Molecules for Organocatalyzed Thioacyl Aminolysis.ACS omega · 2023Article
- An economical approach for peptide synthesisChemical science · 2022Article
- Design of Protein Segments and Peptides for Binding to Protein Targets.Biodesign research · 2022Review
- Geared Toward Applications: A Perspective on Functional Sequence-Controlled Polymers.ACS macro letters · 2021Article
- Proteomimetic surface fragments distinguish targets by function.Chemical science · 2020Article
- Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.Peptide science (Hoboken, N.J.) · 2020Article
- β-Aminopeptidases: Insight into Enzymes without a Known Natural Substrate.Applied and environmental microbiology · 2019Article
- Article
- Sulfono-γ-AA modified peptides that inhibit HIV-1 fusion.Organic & biomolecular chemistry · 2018Article
- Homologation of α-aryl amino acids through quinone-catalyzed decarboxylation/Mukaiyama-Mannich addition.Chemical communications (Cambridge, England) · 2017Article
- Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.Journal of virology · 2017Article
- Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.Angewandte Chemie (International ed. in English) · 2015Review
- Heterogeneous H-bonding in a foldamer helix.Journal of the American Chemical Society · 2015Article
- Positive allostery in metal ion binding by a cooperatively folded β-peptide bundle.Journal of the American Chemical Society · 2014Article
- Molecular architecture with carbohydrate functionalized β-peptides adopting 314-helical conformation.Beilstein journal of organic chemistry · 2014Article
- A β-peptide agonist of the GLP-1 receptor, a class B GPCR.Organic letters · 2013Article
- Plucking the high hanging fruit: a systematic approach for targeting protein-protein interactions.Bioorganic & medicinal chemistry · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Linear peptides derived from the HIV gp41 C-terminus (C-peptides), such as the 36-residue Fuzeon, are potent HIV fusion inhibitors. These molecules bind to the N-peptide region of gp41 and inhibit an intramolecular protein-protein interaction that powers fusion of the viral and host cell membranes. The N-peptide region contains a surface pocket that is occupied in the post-fusion state by three alpha-helical residues found near the gp41 C-terminus: Trp628, Trp631, and Ile635-the WWI epitope. Here, we describe a set of beta3-decapeptides (betaWWI-1-4) in which the WWI epitope is presented on one face of a short 14-helix stabilized by macrodipole neutralization and side chain-side chain salt bridges. betaWWI-1-4 bind in vitro to IZN17, a validated gp41 model, and inhibit syncytia formation in cell culture. Molecules lacking a complete WWI functional epitope neither bind IZN17 nor inhibit syncytia formation. These results provide evidence that short beta-peptide 14-helices can inhibit an intramolecular protein-protein interaction in vivo. Molecules related to betaWWI-1-4 could represent starting points for the development of highly potent inhibitors or antigens effective against HIV or other viruses, including SARS, Ebola, HRSV, and influenza, that employ common fusion mechanisms.
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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.