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Abstract
Key structural features of glucagon-like peptide-1 (GLP-1) analogs may enhance receptor engagement and therapeutic efficacy.
- N-terminal modifications can protect GLP-1 analogs from degradation, potentially increasing their effectiveness.
- C-terminal and backbone elements may stabilize the peptide's structure, improving its affinity for GLP-1 receptors.
- Lipidation and albumin-binding strategies could extend the circulation time of GLP-1 analogs in the body.
- Variations in structure may influence how GLP-1 analogs activate different cellular signaling pathways.
- Emerging multi-receptor agonists are being developed to target a broader range of incretin receptors.
- Computational methods are increasingly applied to optimize the design of peptide therapeutics.
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