ArticleNature communications2019
Peptide-oligourea hybrids analogue of GLP-1 with improved action in vivo.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
28 citing papers in PubMed, 50 citations in OpenAlex.
- Potent and biased agonists of class B1 GPCRs from a heterochiral design strategy.Nature chemistry · 2026Article
- Engineered circular RNA compatible with complete nucleoside modification and rolling circle translation through a Cap-independent translation enhancer.Nature biomedical engineering · 2026Article
- Article
- Optimal Stapling of a Helical Peptide-Foldamer Hybrid Using a C-Terminal 4-Mercaptoproline Enhances Protein Surface Recognition and Cellular Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Synthesis, Characterization, and Antimicrobial Activity of Urea-Containing α/β Hybrid Peptides againstACS omega · 2025Article
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Backbone Modification Provides a Long-Acting Inverse Agonist of Pathogenic, Constitutively Active PTH1R Variants.Journal of the American Chemical Society · 2024Article
- Harnessing Aromatic-Histidine Interactions through Synergistic Backbone Extension and Side Chain Modification.Angewandte Chemie (International ed. in English) · 2023Article
- Hormone Analogues with Unique Signaling Profiles from Replacement of α-Residue Triads with β/γ Diads.Journal of the American Chemical Society · 2023Article
- Design of chimeric GLP-1A using oligomeric bile acids to utilize transporter-mediated endocytosis for oral delivery.Biomaterials research · 2023Article
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 2023Review
- Article
- Sulfono-γ-AApeptides as Protein Helical Domain Mimetics to Manipulate the Angiogenesis.Chembiochem : a European journal of chemical biology · 2022Article
- Helical sulfono-γ-AApeptides with predictable functions in protein recognition.RSC chemical biology · 2022Review
- Rational Design by Structural Biology of Industrializable, Long-Acting Antihyperglycemic GLP-1 Receptor Agonists.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Peptoid-based reprogrammable template for cell-permeable inhibitors of protein-protein interactions.Chemical science · 2021Article
- α/Sulfono-γ-AApeptide Hybrid Analogues of Glucagon with Enhanced Stability and Prolonged In Vivo Activity.Journal of medicinal chemistry · 2021Article
- Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity.Science advances · 2021Article
- Urea-Peptide Hybrids as VEGF-AInternational journal of molecular sciences · 2020Article
- Aromatic Foldamer Helices as α-Helix Extended Surface Mimetics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptides have gained so much attention in the last decade that they are now part of the main strategies, with small molecules and biologics, for developing new medicines. Despite substantial progress, the successful development of peptides as drugs still requires a number of limitations to be addressed, including short in vivo half-lives and poor membrane permeability. Here, we describe the use of oligourea foldamers as tool to improve the pharmaceutical properties of GLP-1, a 31 amino acid peptide hormone involved in metabolism and glycemic control. Our strategy consists in replacing four consecutive amino acids of GLP-1 by three consecutive ureido residues by capitalizing on the structural resemblance of oligourea and α-peptide helices. The efficacy of the approach is demonstrated with three GLP-1-oligourea hybrids showing prolonged activity in vivo. Our findings should enable the use of oligoureas in other peptides to improve their pharmaceutical properties and may provide new therapeutic applications.
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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.