ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structural and biological mimicry of protein surface recognition by alpha/beta-peptide foldamers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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Who cites it
122 citing papers in PubMed.
- Beyond the Active Site: First-In-Class Leishmania Infantum Trypanothione Reductase Dimerization Disruptors as Antileishmanial Leads.ChemMedChem · 2026Review
- De Novo Design of Multivalent α/β-Peptides Mimicking Transcription Factors Targeting the CBP KIX Domain.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Article
- Native Chemical Ligation of Peptoid Oligomers.Biochemistry · 2026Article
- Aromatic Amide Foldamers Show Conformation-Dependent Electronic Properties.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Chemoselective sulfonyl fluoride exchange (SuFEx)-induced macrocyclization of tyrosine-containing peptides in aqueous media.Chemical science · 2025Article
- From Concepts to Inhibitors: A Blueprint for Targeting Protein-Protein Interactions.Chemical reviews · 2025Review
- Article
- Molecular Tweezers Block the Functional Pore of a Protein Machine.Journal of the American Chemical Society · 2025Article
- Harnessing Non-Antibiotic Strategies to Counter Multidrug-Resistant Clinical Pathogens with Special Reference to Antimicrobial Peptides and Their Coatings.Antibiotics (Basel, Switzerland) · 2025Review
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- The Role of Peptides in Combatting HIV Infection: Applications and Insights.Molecules (Basel, Switzerland) · 2024Review
- Site-directed allostery perturbation to probe the negative regulation of hypoxia inducible factor-1α.RSC chemical biology · 2024Article
- In Vitro Selection of Macrocyclic l-α/d-α/β/γ-Hybrid Peptides Targeting IFN-γ/IFNGR1 Protein-Protein Interaction.Journal of the American Chemical Society · 2024Article
- Cyclic βBulletin of the Chemical Society of Japan · 2024Article
- Peptide foldamer-based inhibitors of the SARS-CoV-2 S protein-human ACE2 interaction.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Structural flexibility of apolipoprotein E-derived arginine-rich peptides improves their cell penetration capability.Scientific reports · 2023Article
- Effects of Replacing a Central Glycine Residue in GLP-1 on Receptor Affinity and Signaling Profile.Chembiochem : a European journal of chemical biology · 2023Article
- Harnessing Aromatic-Histidine Interactions through Synergistic Backbone Extension and Side Chain Modification.Angewandte Chemie (International ed. in English) · 2023Article
- Crystal Structure and NMR of an α,δ-Peptide Foldamer Helix Shows Side-Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic.Angewandte Chemie (International ed. in English) · 2023Article
62 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
Abstract
Unnatural oligomers that can mimic protein surfaces offer a potentially useful strategy for blocking biomedically important protein-protein interactions. Here we evaluate an approach based on combining alpha- and beta-amino acid residues in the context of a polypeptide sequence from the HIV protein gp41, which represents an excellent testbed because of the wealth of available structural and biological information. We show that alpha/beta-peptides can mimic structural and functional properties of a critical gp41 subunit. Physical studies in solution, crystallographic data, and results from cell-fusion and virus-infectivity assays collectively indicate that the gp41-mimetic alpha/beta-peptides effectively block HIV-cell fusion via a mechanism comparable to that of gp41-derived alpha-peptides. An optimized alpha/beta-peptide is far less susceptible to proteolytic degradation than is an analogous alpha-peptide. Our findings show how a two-stage design approach, in which sequence-based alpha-->beta replacements are followed by site-specific backbone rigidification, can lead to physical and biological mimicry of a natural biorecognition process.
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