ArticleJournal of the American Chemical Society2014
N-terminal modification of proteins with o-aminophenols.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 119 citations in OpenAlex.
- Exploiting Selective Position Labeling to Unveil the Hidden Complexity of Terminomics.Molecules (Basel, Switzerland) · 2026Review
- Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- Introduction of Reactive Thiol Handles into Tyrosine-Tagged Proteins through Enzymatic Oxidative Coupling.Journal of the American Chemical Society · 2025Article
- Catalysis in Chemical Modification of Proteins.ChemCatChem · 2025Article
- Engineered microbial platform confers resistance against heavy metals via phosphomelanin biosynthesis.Nature communications · 2025Article
- One-Step Purification and N-Terminal Functionalization of Bioactive Proteins via Atypically Split Inteins.Bioconjugate chemistry · 2024Article
- Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins.Molecules (Basel, Switzerland) · 2023Review
- Chemical Conjugation to Less Targeted Proteinogenic Amino Acids.Chembiochem : a European journal of chemical biology · 2022Review
- Tyrosinase-Mediated Synthesis of Nanobody-Cell Conjugates.ACS central science · 2022Article
- A disintegrin derivative as a case study for PHIP labeling of disulfide bridged biomolecules.Scientific reports · 2022Article
- 4-Iodopyrimidine Labeling Reveals Nuclear Translocation and Nuclease Activity for Both MIF and MIF2.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- An overview of chemo- and site-selectivity aspects in the chemical conjugation of proteins.Royal Society open science · 2022Article
- Selective N-Arylation of p-Aminophenylalanine in Unprotected Peptides with Organometallic Palladium Reagents.Angewandte Chemie (International ed. in English) · 2021Article
- Contemporary Approaches for Site-Selective Dual Functionalization of Proteins.Angewandte Chemie (International ed. in English) · 2021Review
- Exploiting Protein N-Terminus for Site-Specific Bioconjugation.Molecules (Basel, Switzerland) · 2021Review
- Linchpins empower promiscuous electrophiles to enable site-selective modification of histidine and aspartic acid in proteins.Chemical science · 2021Article
- One-Step Azolation Strategy for Site- and Chemo-Selective Labeling of Proteins with Mass-Sensitive Probes.Angewandte Chemie (International ed. in English) · 2021Article
- Site-Specific Bioconjugation through Enzyme-Catalyzed Tyrosine-Cysteine Bond Formation.ACS central science · 2020Article
- Copper-mediated peptide arylation selective for the N-terminus.Chemical science · 2020Article
- Secondary modification of oxidatively-modified proline N-termini for the construction of complex bioconjugates.Organic & biomolecular chemistry · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The synthetic modification of proteins plays an important role in chemical biology and biomaterials science. These fields provide a constant need for chemical tools that can introduce new functionality in specific locations on protein surfaces. In this work, an oxidative strategy is demonstrated for the efficient modification of N-terminal residues on peptides and N-terminal proline residues on proteins. The strategy uses o-aminophenols or o-catechols that are oxidized to active coupling species in situ using potassium ferricyanide. Peptide screening results have revealed that many N-terminal amino acids can participate in this reaction, and that proline residues are particularly reactive. When applied to protein substrates, the reaction shows a stronger requirement for the proline group. Key advantages of the reaction include its fast second-order kinetics and ability to achieve site-selective modification in a single step using low concentrations of reagent. Although free cysteines are also modified by the coupling reaction, they can be protected through disulfide formation and then liberated after N-terminal coupling is complete. This allows access to doubly functionalized bioconjugates that can be difficult to access using other methods.
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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.