ArticleChemical science2026
Reprogramming RiPP scaffolds through skeletal editing unlocks chemical space.
Article in Chemical science, 2026. 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.
- Unified Access to Biaryl-Bridged Linkages Unlocks Structural Diversification of Noncanonical Cyclic Peptides.Journal of the American Chemical Society · 2026Article
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Authors and funding
9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In this study, we report (1) a scalable, systematic, and general synthetic approach for the supply of ribosomally synthesized and post-translationally modified peptides (RiPPs) bearing Tyr-Trp cross-linkages, and (2) the comprehensive expansion of novel chemical space through their skeletal diversification. In recent years, numerous biaryl-containing peptides have been discovered, and some of these RiPPs exhibit potent biological activities. However, despite the high metabolic stability and strong target protein binding generally attributed to biaryl RiPPs, their significant strain and rigidity have limited the availability of general synthetic methods. Here, we demonstrate the high versatility of modular synthetic strategies for the construction of RiPPs and achieve the synthesis of a variety of RiPPs containing Tyr-Trp cross-linkages. Furthermore, skeletal diversification
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Registered trials
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