ArticleAngewandte Chemie (International ed. in English)2015
A noncanonical function of sortase enables site-specific conjugation of small molecules to lysine residues in proteins.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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
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Who cites it
24 citing papers in PubMed, 56 citations in OpenAlex.
- Highly Efficient Transpeptidase-Catalyzed Isopeptide Ligation.Journal of the American Chemical Society · 2025Article
- Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.Chembiochem : a European journal of chemical biology · 2024Article
- SpSrtA-Catalyzed Isopeptide Ligation on Lysine Residues.Microorganisms · 2024Article
- Enzymatic Protein Immobilization for Nanobody Array.Molecules (Basel, Switzerland) · 2024Article
- An injectable PEG-like conjugate forms a subcutaneous depot and enables sustained delivery of a peptide drug.Biomaterials · 2023Article
- Peptide/protein-based macrocycles: from biological synthesis to biomedical applications.RSC chemical biology · 2022Review
- Site-selective lysine conjugation methods and applications towards antibody-drug conjugates.Chemical communications (Cambridge, England) · 2021Review
- Enzymatic Methods for the Site-Specific Radiolabeling of Targeting Proteins.Molecules (Basel, Switzerland) · 2021Review
- DNAzymes for amine and peptide lysine acylation.Organic & biomolecular chemistry · 2021Article
- Lysine acylation using conjugating enzymes for site-specific modification and ubiquitination of recombinant proteins.Nature chemistry · 2020Article
- Kinetics and Optimization of the Lysine-Isopeptide Bond Forming Sortase Enzyme fromBioconjugate chemistry · 2020Article
- Recent trends in protein and peptide-based biomaterials for advanced drug delivery.Advanced drug delivery reviews · 2020Review
- Broadening the scope of sortagging.RSC advances · 2019Review
- Recent progress in enzymatic protein labelling techniques and their applications.Chemical Society reviews · 2018Review
- In Situ Cyclization of Native Proteins: Structure-Based Design of a Bicyclic Enzyme.Angewandte Chemie (International ed. in English) · 2018Article
- Protein Labeling via a Specific Lysine-Isopeptide Bond Using the Pilin Polymerizing Sortase from Corynebacterium diphtheriae.Journal of the American Chemical Society · 2018Article
- Sortase-Mediated Ligation as a Modular Approach for the Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22 Virus-like Particle.Bioconjugate chemistry · 2017Article
- Proximity-Based Sortase-Mediated Ligation.Angewandte Chemie (International ed. in English) · 2017Article
- Encapsulating a Hydrophilic Chemotherapeutic into Rod-like Nanoparticles of a Genetically Encoded Asymmetric Triblock Polypeptide Improves its Efficacy.Advanced functional materials · 2017Article
- Site-Specific and Stoichiometric Stealth Polymer Conjugates of Therapeutic Peptides and Proteins.Bioconjugate chemistry · 2017Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We provide the first demonstration that isopeptide ligation, a noncanonical activity of the enzyme sortase A, can be used to modify recombinant proteins. This reaction was used in vitro to conjugate small molecules to a peptide, an engineered targeting protein, and a full-length monoclonal antibody with an exquisite level of control over the site of conjugation. Attachment to the protein substrate occurred exclusively through isopeptide bonds at a lysine ε-amino group within a specific amino acid sequence. This reaction allows more than one molecule to be site-specifically conjugated to a protein at internal sites, thereby overcoming significant limitations of the canonical native peptide ligation reaction catalyzed by sortase A. Our method provides a unique chemical ligation procedure that is orthogonal to existing methods, supplying a new method to site-specifically modify lysine residues that will be a valuable addition to the protein conjugation toolbox.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.