ArticleJournal of the American Chemical Society2020
Genetically Encoded Quinone Methides Enabling Rapid, Site-Specific, and Photocontrolled Protein Modification with Amine Reagents.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Recent advances in site-specific modifications of peptides and proteins.Chemical science · 2026Review
- Molecular Design Strategies Enabling Activity-Based Sensing and Labeling as a Platform for Probing Enzyme Activity, Redox Regulation, and Transition-Metal Signaling.Bioconjugate chemistry · 2026Review
- Reactivity of δ-Functionalized Para-Quinone Methides in Nucleophilic Addition Reactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Terminal spin labeling of xylotriose strongly affects interactions in the active site of xylanase BcX.Journal of biomolecular NMR · 2025Article
- A hydrophobic photouncaging reaction to profile the lipid droplet interactome in tissues.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion.Chemical reviews · 2024Review
- Biospecific Chemistry for Covalent Linking of Biomacromolecules.Chemical reviews · 2024Review
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Advancing protein therapeutics through proximity-induced chemistry.Cell chemical biology · 2024Review
- Structural Determinants of Stimuli-Responsiveness in Amphiphilic Macromolecular Nano-assemblies.Progress in polymer science · 2024Article
- Novel Derivatives of Nitrobenzofurazan with Chromogenic and Fluorogenic Properties.Molecules (Basel, Switzerland) · 2023Article
- Ultrafast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids.Journal of the American Chemical Society · 2023Article
- Residue selective crosslinking of proteins through photoactivatable or proximity-enabled reactivity.Current opinion in chemical biology · 2023Review
- Genetically encoded crosslinkers to address protein-protein interactions.Protein science : a publication of the Protein Society · 2023Review
- Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023Review
- Split aminoacyl-tRNA synthetases for proximity-induced stop codon suppression.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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Authors and funding
10 authors.
Funding
Abstract
Site-specific modification of proteins with functional molecules provides powerful tools for researching and engineering proteins. Here we report a new chemical conjugation method which photocages highly reactive but chemically selective moieties, enabling the use of protein-inert amines for selective protein modification. New amino acids FnbY and FmnbY, bearing photocaged quinone methides (QMs), were genetically incorporated into proteins. Upon light activation, they generated highly reactive QM, which rapidly reacted with amine derivatives. This method features a rare combination of desired properties including fast kinetics, small and stable linkage, compatibility with low temperature, photocontrollability, and widely available reagents. Moreover, labeling via FnbY occurs on the β-carbon, affording the shortest linkage to protein backbone which is essential for advanced studies involving orientation and distance. We installed various functionalities onto proteins and attached a spin label as close as possible to the protein backbone, achieving high resolution in double electron-electron paramagnetic resonance distance measurements.
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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.