ArticleJournal of the American Chemical Society2013
Simultaneous dual protein labeling using a triorthogonal reagent.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Farnesyltransferase Enables Modular Assembly of Dual-Functional Nanobody Conjugates for in Vivo Imaging of Inflammation.Angewandte Chemie (International ed. in English) · 2026Article
- Scalable Flow Synthesis of Genetically Encodable Tetrazine Amino Acids.Organic process research & development · 2026Article
- Engineering protein prenylation: an emerging tool for selective protein modification.Biochemical Society transactions · 2025Review
- Targeted Drug Delivery by MMAE Farnesyl-Bioconjugated Multivalent Chemically Self-Assembled Nanorings Induces Potent Receptor-Dependent Immunogenic Cell Death.Bioconjugate chemistry · 2024Article
- Bioorthogonal labeling and profiling of N6-isopentenyladenosine (i6A) modified RNA.Nucleic acids research · 2024Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Review
- Site-specific dual encoding and labeling of proteins via genetic code expansion.Cell chemical biology · 2023Review
- Engineering Biomimetic Trogocytosis with Farnesylated Chemically Self-Assembled Nanorings.Biomacromolecules · 2022Article
- Manipulating Cell Fates with Protein Conjugates.Bioconjugate chemistry · 2022Review
- Bivalent EGFR-Targeting DARPin-MMAE Conjugates.International journal of molecular sciences · 2022Article
- Synthesis of cholera toxin B subunit glycoconjugates using site-specific orthogonal oxime and sortase ligation reactions.Frontiers in chemistry · 2022Article
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Contemporary Approaches for Site-Selective Dual Functionalization of Proteins.Angewandte Chemie (International ed. in English) · 2021Review
- Bifunctional Reagents for Formylglycine Conjugation: Pitfalls and Breakthroughs.Chembiochem : a European journal of chemical biology · 2020Article
- Engineering reversible cell-cell interactions using enzymatically lipidated chemically self-assembled nanorings.Chemical science · 2020Article
- Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System.Frontiers in bioengineering and biotechnology · 2020Article
- ChemoenzymaticJournal of the American Chemical Society · 2019Article
- Recent progress in enzymatic protein labelling techniques and their applications.Chemical Society reviews · 2018Review
- Metabolic Labeling of Prenylated Proteins Using Alkyne-Modified Isoprenoid Analogues.Current protocols in chemical biology · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
Construction of heterofunctional proteins is a rapidly emerging area of biotherapeutics. Combining a protein with other moieties, such as a targeting element, a toxic protein or small molecule, and a fluorophore or polyethylene glycol (PEG) group, can improve the specificity, functionality, potency, and pharmacokinetic profile of a protein. Protein farnesyl transferase (PFTase) is able to site-specifically and quantitatively prenylate proteins containing a C-terminal CaaX-box amino acid sequence with various modified isoprenoids. Here, we describe the design, synthesis, and application of a triorthogonal reagent, 1, that can be used to site-specifically incorporate an alkyne and aldehyde group simultaneously into a protein. To illustrate the capabilities of this approach, a protein was enzymatically modified with compound 1 followed by oxime ligation and click reaction to simultaneously incorporate an azido-tetramethylrhodamine (TAMRA) fluorophore and an aminooxy-PEG moiety. This was performed with both a model protein [green fluorescent protein (GFP)] as well as a therapeutically useful protein [ciliary neurotrophic factor (CNTF)]. Next, a protein was enzymatically modified with compound 1 followed by coupling to an azido-bis-methotrexate dimerizer and aminooxy-TAMRA. Incubation of that construct with a dihydrofolate reductase (DHFR)-DHFR-anti-CD3 fusion protein resulted in the self-assembly of nanoring structures that were endocytosed into T-leukemia cells and visualized therein. These results highlight how complex multifunctional protein assemblies can be prepared using this facile triorthogonal approach.
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