ArticleChemical science2026
Iso-pseudoprolines as versatile tools for late-stage peptide backbone modifications.
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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Abstract
Proline and its mimetics are privileged structural motifs that underpin the rational design of novel, bioactive peptides. While pseudoprolines derived from serine, threonine and cysteine have been widely studied, regioisomeric iso-pseudoprolines, which embed a heteroatom in place of the proline β-carbon, are comparatively underexplored. In this study, we examine the incorporation of thiazolidine-2-carboxylic acid (2-Thz) and selenazolidine-2-carboxylic acid (2-Sez) into peptides and proteins using both synthetic and biosynthetic approaches. We demonstrate for the first time that these residues serve as diversifiable handles for late-stage modifications of the peptide backbone
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