Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 140, Issue 24, Pages 7381-7384Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b02176
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Funding
- National Science Foundation [CHE-1565520]
- STF at the University of Washington
- Burroughs Wellcome Fund Career Award at the Scientific Interface
- Paul Berg Early Career Professorship
- Lloyd and Dottie Huck Early Career Award
- National Institutes of Health [R01 GM121858]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1565520] Funding Source: National Science Foundation
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We present a fluorogenic method to visualize misfolding and aggregation of a specific proteinof-interest in live cells using structurally modulated fluorescent protein chromophores. Combining photophysical analysis, X-ray crystallography, and theoretical calculation, we show that fluorescence is triggered by inhibition of twisted-intramolecular charge transfer of these fluorophores in the rigid microenvironment of viscous solvent or protein aggregates. Bioorthogonal conjugation of the fluorophore to Halo-tag fused protein-of-interests allows for fluorogenic detection of both misfolded and aggregated species in live cells. Unlike other methods, our method is capable of detecting previously invisible misfolded soluble proteins. This work provides the first application of fluorescent protein chromophores to detect protein conformational collapse in live cells.
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