Evidence map›Paper›PMID 32440547›Full record

ArticleScience advances2020

The activity of sulfono-γ-AApeptide helical foldamers that mimic GLP-1.

Peng Sang, Zhihong Zhou, Yan Shi, Candy Lee, Zaid Amso, David Huang, Timothy Odom, Vân T B Nguyen-Tran, Weijun Shen, Jianfeng Cai

Abstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Helical sulfonyl-γ-AApeptides modulating Aβ oligomerization and cytotoxicity by recognizing Aβ helix.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Acta pharmaceutica Sinica. B · 2023
    Article
  15. Sulfono-γ-AApeptides as Protein Helical Domain Mimetics to Manipulate the Angiogenesis.Chembiochem : a European journal of chemical biology · 2022
    Article
  16. Article
  17. Review
  18. Statistic Copolymers Working as Growth Factor-Binding Mimics of Fibronectin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Peng SangDepartment of Chemistry, University of South Florida, 4202 E. Fowler Ave., Tampa, FL 33620, USA.ORCID 0000-0002-8336-4533
Zhihong ZhouCalibr at Scripps Research, 11119 N. Torrey Pines Rd., La Jolla, CA 92037, USA.ORCID 0000-0001-5036-496X
Yan ShiDepartment of Chemistry, University of South Florida, 4202 E. Fowler Ave., Tampa, FL 33620, USA.ORCID 0000-0002-4086-6103
Candy LeeCalibr at Scripps Research, 11119 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Zaid AmsoCalibr at Scripps Research, 11119 N. Torrey Pines Rd., La Jolla, CA 92037, USA.ORCID 0000-0002-8724-2445
David HuangCalibr at Scripps Research, 11119 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Timothy OdomDepartment of Chemistry, University of South Florida, 4202 E. Fowler Ave., Tampa, FL 33620, USA.
Vân T B Nguyen-TranCalibr at Scripps Research, 11119 N. Torrey Pines Rd., La Jolla, CA 92037, USA.ORCID 0000-0001-5678-1908
Weijun ShenCalibr at Scripps Research, 11119 N. Torrey Pines Rd., La Jolla, CA 92037, USA.ORCID 0000-0001-8388-729X
Jianfeng CaiDepartment of Chemistry, University of South Florida, 4202 E. Fowler Ave., Tampa, FL 33620, USA.ORCID 0000-0003-3106-3306

Funding

Requesting HPLC for the project of "Alpha-AApeptides as a Novel Class of Antimicrobial Biomaterials"R01GM112652 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI CAI, JIANFENG · 2015 to 2019
$1.5M
NIGMS NIH HHS R01 GM112652
6 · The paper itself

Abstract

Existing long α-helix mimicking necessitates the retention of most natural amino acid residues to maintain their biological activity. Here, we report the exploration of helical sulfono-γ-AApeptides with entire unnatural backbones for their ability to structurally and functionally mimic glucagon-like peptide 1 (GLP-1). Our findings suggest that efficient construction of novel GLP-1 receptor (GLP-1R) agonists could be achieved with nanomolar potencies. In addition, the resulting sulfono-γ-AApeptides were also proved to display remarkable stability against enzymatic degradation compared to GLP-1, augmenting their biological potential. This alternative strategy of α-helix mimicking, as a proof of concept, could provide a new paradigm to prepare GLP-1R agonists.

Indexed as

Glucagon-Like Peptide 1PeptidomimeticsPeptidesProtein Conformation, alpha-HelicalGlucagon-Like Peptide 1PeptidesPeptidomimetics

Identifiers

PMID32440547
PMCPMC7228743

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Registered trials

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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.