Abstract
Glucagon-like peptide-1 receptor (GLP-1R) ligands including semaglutide play an important role in drug discovery. Herein, a short semaglutide-derived GLP-1R-engaging segment was used as the basis for scaffold construction, and conformational restabilisation was introduced through lactam stapling and bulky aromatic non-natural amino acid substitution. A total of 108 stapled peptide candidates were designed by structure-guided modelling and virtual screening. Among them, 35 peptides were synthesised and characterised. Most stapled analogues showed improved serum and proteolytic stability relative to semaglutide, and 11CP-17B, 11CP-17N, and 11CP-19N showed the most favourable stability profiles. Molecular dynamics simulations and MM-GBSA analysis were consistent with receptor-compatible poses and favourable predicted interaction patterns for these representative analogues. Collectively, these results define a practical strategy for constructing stabilised semaglutide-derived peptide scaffolds and provide a basis for subsequent functional optimisation of GLP-1R-targeting peptides.
| Original language | English |
|---|---|
| Pages (from-to) | 2714331 |
| Number of pages | 1 |
| Journal | Journal of Enzyme Inhibition and Medicinal Chemistry |
| Volume | 41 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1 Dec 2026 |
Keywords
- GLP-1R
- peptide scaffolds
- peptide stability
- Semaglutide
- stapled peptides
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