Structural Dynamics of GLP-1 Analogues: Folding Energetics, Lipidation-Driven Assembly, and Aggregation Mechanisms
Angelo Santoro, Marco Macis, Anna Maria D’Ursi, Antonio Ricci · 2026
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Description
Angelo Santoro and co-authors examine in 2026 the restless structures of GLP-1 analogues, the peptide drugs now central to diabetes and obesity care. These peptides do not sit in one shape. They fold, pair up, clump, and bind to blood albumin in competing equilibria. Those equilibria decide both how long they last and whether they stay intact. The study analyzes how sequence tweaks and fatty lipid attachments shift that balance.
Helix-promoting residues and backbone constraints steady the folded form, while lipidation creates the albumin-bound state that prolongs action but also invites assembly and aggregation. Salt levels, temperature, and even manufacturing steps act as perturbations that can disturb structural integrity. New multi-agonist peptides, which hit several hormone receptors at once, widen the shape diversity further and strain existing design methods. The authors argue predictive models must treat folding and aggregation as one coupled problem.
Catalog record
| CREATOR | Angelo Santoro, Marco Macis, Anna Maria D’Ursi, Antonio Ricci |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 34969 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |