ArticleJournal of the American Chemical Society2012
Enhancement of α-helix mimicry by an α/β-peptide foldamer via incorporation of a dense ionic side-chain array.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed.
- Article
- Chemoselective sulfonyl fluoride exchange (SuFEx)-induced macrocyclization of tyrosine-containing peptides in aqueous media.Chemical science · 2025Article
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Differential membrane binding of α/β-peptide foldamers: implications for cellular delivery and mitochondrial targeting.Australian journal of chemistry · 2023Article
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 2023Review
- Oligoarginine-Conjugated Peptide Foldamers Inhibiting Vitamin D Receptor-Mediated Transcription.ACS omega · 2022Article
- Design and Engineering of Miniproteins.ACS bio & med chem Au · 2022Review
- A Modular Synthesis of Teraryl-Based α-Helix Mimetics, Part 3: Iodophenyltriflate Core Fragments Featuring Side Chains of Proteinogenic Amino Acids.European journal of organic chemistry · 2022Article
- The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness.Communications chemistry · 2021Article
- Engineering Protease-Resistant Peptides to Inhibit Human Parainfluenza Viral Respiratory Infection.Journal of the American Chemical Society · 2021Article
- A Triptycene-Based Enantiopure Bis(Diazadibenzoanthracene) by a Chirality-Assisted Synthesis Approach.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Effects of Single α-to-β Residue Replacements on Recognition of an Extended Segment in a Viral Fusion Protein.ACS infectious diseases · 2020Article
- Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Chembiochem : a European journal of chemical biology · 2018Article
- Impact of Backbone Pattern and Residue Substitution on Helicity in α/β/γ-Peptides.Journal of the American Chemical Society · 2018Article
- Development of Potent, Protease-Resistant Agonists of the Parathyroid Hormone Receptor with Broad β Residue Distribution.Journal of medicinal chemistry · 2017Article
- Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF.Chembiochem : a European journal of chemical biology · 2017Article
- Backbone Modification of a Parathyroid Hormone Receptor-1 Antagonist/Inverse Agonist.ACS chemical biology · 2016Article
- Targeting recognition surfaces on natural proteins with peptidic foldamers.Current opinion in structural biology · 2016Review
- Folding and function in α/β-peptides: targets and therapeutic applications.Current opinion in chemical biology · 2015Review
- Multi-Facial, Non-Peptidic α-Helix Mimetics.Biology · 2015Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
We report a new method for preorganization of α/β-peptide helices, based on the use of a dense array of acidic and basic side chains. Previously we have used cyclically constrained β residues to promote α/β-peptide helicity; here we show that an engineered ion pair array can be comparably effective, as indicated by mimicry of the CHR domain of HIV protein gp41. The new design is effective in biochemical and cell-based infectivity assays; however, the resulting α/β-peptide is susceptible to proteolysis. This susceptibility was addressed via introduction of a few cyclic β residues near the cleavage site, to produce the most stable, effective α/β-peptide gp41 CHR analogue identified. Crystal structures of an α- and α/β-peptide (each involved in a gp41-mimetic helix bundle) that contain the dense acid/base residue array manifest disorder in the ionic side chains, but there is little side-chain disorder in analogous α- and α/β-peptide structures with a sparser ionic side-chain array. These observations suggest that dense arrays of complementary acidic and basic residues can provide conformational stabilization via Coulombic attractions that do not require entropically costly ordering of side chains.
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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.