ArticleNature chemical biology2026
Real-time imaging of protein microenvironment changes in cells with rotor-based fluorescent amino acids.
Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Design, Synthesis, and Applications of Fluorescent Amino Acids in Bioimaging.Chemical & biomedical imaging · 2026Review
- Structural Control of Dual Emission in Coumarin Fluorophores for Visualizing Protein Droplet Maturation.Angewandte Chemie (International ed. in English) · 2026Article
- Real-Time Detection of Burn Wound Infection via a Turn-On NIR-II Fluorescent Probe.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Molecular Interactions of Resistant Dextrin with Wheat Starch and Gluten: Structural Dynamics and Macromolecular Network Formation.Foods (Basel, Switzerland) · 2026Article
- Molecular rotor-based probes for protein monitoring in biomedical research.Nature reviews. Chemistry · 2026Review
- Sequence Display enables large-scale sequence-activity datasets for rapid protein evolution.Nature biotechnology · 2026Article
- Sweetening ferroptosis spread.Nature chemical biology · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
Fluorescent protein fusions with environmentally sensitive fluorophores have been widely used to investigate changes in the protein microenvironment. Unfortunately, these techniques often rely on bulky fluorescent proteins or tags to the N terminus or C terminus of the target protein, which can disrupt the behavior of the target protein and may limit their ability to investigate microenvironment changes with high spatial resolution. Here we develop a strategy to visualize microenvironment changes of protein substructures in real time by genetically incorporating environment-sensitive noncanonical amino acids (ncAAs) containing rotor-based fluorophores at specific positions of the target protein. Through computational redesign of aminoacyl-tRNA synthetase, we successfully incorporated these rotor-based ncAAs into several proteins in mammalian cells. Precise placement of these ncAAs at specific sites of proteins enables the detection of microenvironmental changes around individual residues during events such as aggregation, clustering, cluster dissociation and others.
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Registered trials
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