ArticleJournal of peptide science : an official publication of the European Peptide Society2025
Helicity-Dependent Enzymatic Peptide Cyclization.
Article in Journal of peptide science : an official publication of the European Peptide Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Peptidomics-guided 3D structural-mechanistic investigation of bovine colostrum peptides reveals multi-targetedFood chemistry: X · 2026Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The secondary structure plays a crucial role in the biological activity of peptides. Various strategies have been developed to stabilize particular peptide conformations, including sequence modifications and macrocyclization approaches. Often, the interplay between conformational constraint and flexibility is central to bioactivity. Here, we investigate how peptide α-helicity influences enzymatic head-to-tail cyclization using an engineered Sortase. We show that peptides with low helicity readily undergo intramolecular cyclization, while more rigid, helical peptides exhibit complex cyclization behaviors including cyclic dimer formation. These findings reveal that increased peptide rigidity can redirect enzymatic reactions from intramolecular to intermolecular processes, and demonstrates how changes in molecular rigidity can guide chemical reactivity. These insights can advance the design of peptide-derived materials, hydrogels, and stimuli-responsive probes.
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Registered trials
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