ArticleACS omega2025
Rational Activity Improvement of Cyclic Peptides through Stabilization and Rigidification of Main Chain Using φ/ψ Plots of Amino Acids.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- The fourth controlled release society workshop on oral peptide administration.Frontiers in drug delivery · 2026Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Medium-sized cyclic peptides that target challenging protein-protein interactions are promising as a new therapeutic modality. To enhance activity, rigidifying the bioactive conformation of these peptides has a great opportunity due to their higher number of rotatable bonds compared with small molecules. In this study, we classified 36 types of α-amino acids (natural and non-natural) and calculated their φ/ψ free energy maps and main chain torsional entropy, a measure of rigidity, for each category. By comparing the φ/ψ torsional angles from the X-ray structure of the hit peptide AP0343 with the computed φ/ψ maps, we demonstrated that the main chain structure could be rationally rigidified. We validated this approach for the derivatization of AP0343 to the clinical KRAS inhibitor LUNA18 and confirmed its utility in an actual drug discovery project. This method is effective for optimizing main chain structures and advancing orally available medium-sized cyclic peptides.
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Registered trials
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