ArticleChemistry (Weinheim an der Bergstrasse, Germany)2026
Chemical Ligation of Backbone N-hydroxylated Peptides.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 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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1 citing paper in PubMed.
- Backbone N-heteroatom substitution as a strategy to enhance peptide proteolytic stability.RSC chemical biology · 2026Article
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2 authors.
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Abstract
Hydroxamate groups provide a unique opportunity to promote amide-bond formation between unprotected peptide fragments through intramolecular O-acyl capture and O→N acyl transfer. Here, we report a general ligation strategy that exploits the reactivity of backbone N-hydroxy peptide (NHP) fragments to achieve efficient couplings with peptide thioesters in aqueous buffer. NHP ligation is broadly compatible with β-branched, aromatic, charged, and N-methylated residues at the nucleophilic N-terminus. Preparative-scale ligation and subsequent N─O bond reduction furnish products with a restored native peptide bond. The versatility of this method is demonstrated through the convergent synthesis of two miniproteins whose folding and thermal stability are modulated by backbone N-hydroxylation, and in the synthesis of the macrocyclic NHP natural product talarolide A. These studies establish backbone NHP ligation as a robust and widely applicable strategy for peptide and protein synthesis.
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