ArticleAngewandte Chemie (International ed. in English)2022
Sortase-Mediated Multi-Fragment Assemblies by Ligation Site Switching.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- Coil-Tag Conjugation: A Next Gen Site-Specific ADC Fabrication Technology.Bioconjugate insights · 2026Article
- Photocontrolled Reversible Amyloid Fibril Formation of Parathyroid Hormone-Derived Peptides.Bioconjugate chemistry · 2024Article
- Sortase-mediated labeling: Expanding frontiers in site-specific protein functionalization opens new research avenues.Current opinion in chemical biology · 2024Review
- Microbial Synthesis of High-Molecular-Weight, Highly Repetitive Protein Polymers.International journal of molecular sciences · 2023Review
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Sortase-Mediated Multi-Fragment Assemblies by Ligation Site Switching.Angewandte Chemie (International ed. in English) · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Sortase-mediated ligation (SML) is a powerful tool of protein chemistry allowing the ligation of peptides containing LPxTG sorting motifs and N-terminal glycine nucleophiles. The installation of a sorting motif into the product prohibits the assembly of multiple fragments by SML. Here we report multi-fragment SML based on switchable sortase substrates. Substitution of the Leu residue by disulfide-containing Cys(StBu) results in active sorting motifs, which are inactivatable by reduction. In combination with a photo-protected N-Gly nucleophile, multi-fragment SML is enabled by repetitive cycles of SML and ligation site switching. The feasibility of this approach was demonstrated by a proof-of-concept four-fragment ligation, the assembly of peptide probes for bivalent chromatin binding proteins and oligomerization of peptide antigens. Biochemical and immuno-assays demonstrated functionality of these probes rendering them promising tools for immunology and chromatin biochemistry.
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Registered trials
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