ArticleNature chemistry2024
Designing artificial fluorescent proteins and biosensors by genetically encoding molecular rotor-based amino acids.
Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Design, Synthesis, and Applications of Fluorescent Amino Acids in Bioimaging.Chemical & biomedical imaging · 2026Review
- Molecular rotor-based probes for protein monitoring in biomedical research.Nature reviews. Chemistry · 2026Review
- Recoding multiple rare codons enables the simultaneous incorporation of up to five distinct noncanonical amino acids.Nature chemistry · 2026Article
- Fluorogenic Covalent Probes for RNA.Journal of the American Chemical Society · 2025Article
- A twisted chromophore powers a turn-on fluorescent protein chloride sensor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Respiration Drives Dynamic Metal-Organic Framework for Smart Photoresponse to Volatile Toxic Vapors and Their Photodynamic Sterilization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mimicking fluorophores from nature to generate artificial fluorescent proteins and biosensors.Nature chemistry · 2024Article
- Catalysis-enabled amine sorting.Nature chemistry · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Fluorescent proteins are indispensable tools in biological and medical research. The fluorophores are typically encoded by the primary amino acid sequence, from which a fluorescent molecular rotor structure forms upon protein folding. Here, inspired by the fluorogenic property exhibited by native fluorophores, we designed a collection of fluorogenic non-canonical amino acids that feature this molecular rotor structure-termed fluorescent molecular rotor amino acids (FMR-AAs)-akin to native fluorescent protein fluorophores. By incorporating FMR-AAs into target proteins through an expanded genetic code, we use them as encoded fluorophore analogues within a confined protein microenvironment, thus readily transforming diverse non-fluorescent proteins into artificial fluorescent proteins. We also use FMR-AAs in selected proteins as sensitive fluorescent probes for monitoring protein-protein interactions and detecting protein conformational changes in vitro and in living cells. This approach enables the generation of artificial fluorescent proteins and the development of biosensors from potentially any protein of interest with minor modifications.
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Registered trials
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