ArticleBiophysical journal2023
Glucagon-like peptide 1 aggregates into low-molecular-weight oligomers off-pathway to fibrillation.
Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed.
- Anisotropic Electrostatics in the Instability of GLP‑1 Analog Micelles: Effects of Electrolytes, Denaturants, pH, and Temperature.ACS omega · 2026Article
- Analytical Ultracentrifugation for Biopharmaceutical Characterization and Quality Control.International journal of molecular sciences · 2026Review
- Fibrillar and Micellar Aggregation of Semaglutide and Formation of a Chiral-Imprinted Glass.Biomacromolecules · 2026Article
- Cosolute effects reveal the nature of weak forces governing GLP-1 oligomer stability.The Journal of biological chemistry · 2026Article
- Dissecting Hidden Liraglutide Oligomerization Pathways via Direct Mass Technology, Electron-Capture Dissociation, and Molecular Dynamics.Analytical chemistry · 2025Article
- Incretins and MASLD: at the Crossroads of Endocrine and Hepatic Disorders.Current obesity reports · 2025Review
- Semaglutide Aggregates into Oligomeric Micelles and Short Fibrils in Aqueous Solution.Biomacromolecules · 2025Article
- Eliminating viscosity challenges in continuous cultivation of yeast producing a GLP-1 like peptide.Microbial cell factories · 2025Article
- Interaction Between Glucagon-like Peptide 1 and Its Analogs with Amyloid-β Peptide Affects Its Fibrillation and Cytotoxicity.International journal of molecular sciences · 2025Article
- Effect of Lipidation on the Structure, Oligomerization, and Aggregation of Glucagon-like Peptide 1.Bioconjugate chemistry · 2025Article
- A miniature low-immunogenic platform for the biosynthesis of self-assembling protein nanoparticles.Nanotheranostics · 2025Article
- Machine-Learning-Guided Peptide Drug Discovery: Development of GLP-1 Receptor Agonists with Improved Drug Properties.Journal of medicinal chemistry · 2024Article
- Energy Landscapes and Structural Ensembles of Glucagon-like Peptide-1 Monomers.The journal of physical chemistry. B · 2024Article
- Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation.Chemical science · 2024Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The physical stability of peptide-based drugs is of great interest to the pharmaceutical industry. Glucagon-like peptide 1 (GLP-1) is a 31-amino acid peptide hormone, the analogs of which are frequently used in the treatment of type 2 diabetes. We investigated the physical stability of GLP-1 and its C-terminal amide derivative, GLP-1-Am, both of which aggregate into amyloid fibrils. While off-pathway oligomers have been proposed to explain the unusual aggregation kinetics observed previously for GLP-1 under specific conditions, these oligomers have not been studied in any detail. Such states are important as they may represent potential sources of cytotoxicity and immunogenicity. Here, we identified and isolated stable, low-molecular-weight oligomers of GLP-1 and GLP-1-Am, using size-exclusion chromatography. Under the conditions studied, isolated oligomers were shown to be resistant to fibrillation or dissociation. These oligomers contain between two and five polypeptide chains and they have a highly disordered structure as indicated by a variety of spectroscopic techniques. They are highly stable with respect to time, temperature, or agitation despite their noncovalent character, which was established using liquid chromatography-mass spectrometry and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These results provide evidence of stable, low-molecular-weight oligomers that are formed by an off-pathway mechanism which competes with amyloid fibril formation.
Indexed as
Identifiers
What OpenQuestion holds
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.