ArticleBiophysical journal2015
Oligomerization of a Glucagon-like Peptide 1 Analog: Bridging Experiment and Simulations.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 60 citations in OpenAlex.
- An Orthogonal Framework for Higher-Order Structural and In Vitro Functional Comparability of Chemically Synthesized Liraglutide Relative to an rDNA-Origin Reference Product.Pharmaceutical research · 2026Article
- Anisotropic Electrostatics in the Instability of GLP‑1 Analog Micelles: Effects of Electrolytes, Denaturants, pH, and Temperature.ACS omega · 2026Article
- Structural Dynamics of GLP-1 Analogues: Folding Energetics, Lipidation-Driven Assembly, and Aggregation Mechanisms.Molecules (Basel, Switzerland) · 2026Review
- Simple Hydrodynamic Molecular Weight Model for Rapid Assessment of Therapeutic Protein Oligomerization States in Formulation.The AAPS journal · 2026Article
- Methyl Proton Spin Relaxation (Analytical chemistry · 2026Article
- Cosolute effects reveal the nature of weak forces governing GLP-1 oligomer stability.The Journal of biological chemistry · 2026Article
- Self-Assembly of a Therapeutic Peptide Surfactant: A Small-Angle X-ray Scattering Study.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Effect of a Low Electrostatic Environment on the Helical Structures of Peptides and Proteins Using Flexible Water Models: An In Silico Study.ACS omega · 2025Article
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- Revealing Anisotropic Growth of Liraglutide Oligomers by Native Ion Mobility Mass Spectrometry and Molecular Dynamics Simulation.ACS central science · 2025Article
- Dissecting Hidden Liraglutide Oligomerization Pathways via Direct Mass Technology, Electron-Capture Dissociation, and Molecular Dynamics.Analytical chemistry · 2025Article
- Article
- A Robust Platform for the Molecular Design of Potent, Protease-Stable, Long-Acting GIP Analogues.Journal of medicinal chemistry · 2024Article
- Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids.Nature communications · 2023Article
- A Spectroscopic and Molecular Dynamics Study on the Aggregation Properties of a Lipopeptide Analogue of Liraglutide, a Therapeutic Peptide against Diabetes Type 2.Molecules (Basel, Switzerland) · 2023Article
- Field-Flow Fractionation in Molecular Biology and Biotechnology.Molecules (Basel, Switzerland) · 2023Review
- Direct Assessment of Oligomerization of Chemically Modified Peptides and Proteins in Formulations using DLS and DOSY-NMR.Pharmaceutical research · 2023Article
- Intestinal epithelium penetration of liraglutide via cholic acid pre-complexation and zein/rhamnolipids nanocomposite delivery.Journal of nanobiotechnology · 2023Article
- GLP-1R Signaling and Functional Molecules in Incretin Therapy.Molecules (Basel, Switzerland) · 2023Review
- Application of Af4-Multidetection to Liraglutide in Its Formulation: Preserving and Representing Native Aggregation.Molecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glucagon-like peptide 1 (GLP-1) analog, liraglutide, is a GLP-1 agonist and is used in the treatment of type-2 diabetes mellitus and obesity. From a pharmaceutical perspective, it is important to know the oligomerization state of liraglutide with respect to stability. Compared to GLP-1, liraglutide has an added fatty acid (FA) moiety that causes oligomerization of liraglutide as suggested by small-angle x-ray scattering (SAXS) and multiangle static light scattering (MALS) results. SAXS data suggested a global shape of a hollow elliptical cylinder of size hexa-, hepta-, or octamer, whereas MALS data indicate a hexamer. To elaborate further on the stability of these oligomers and the role of the FA chains, a series of molecular-dynamics simulations were carried out on 11 different hexa-, hepta-, and octameric systems. Our results indicate that interactions of the fatty acid chains contribute noticeably to the stabilization. The simulation results indicate that the heptamer with paired FA chains is the most stable oligomer when compared to the 10 other investigated structures. Theoretical SAXS curves extracted from the simulations qualitatively agree with the experimentally determined SAXS curves supporting the view that liraglutide forms heptamers in solution. In agreement with the SAXS data, the heptamer forms a water-filled oligomer of elliptical cylindrical shape.
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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.