Presentation
13 March 2024 Magnetic control of GFP-like fluorescent proteins
Author Affiliations +
Abstract
We've discovered a simple, nontoxic, biocompatible way to control the brightness of GFP-like fluorescent proteins via modest magnetic fields (~10 mT). Fluorescent proteins which seem magnetically inert (e.g. EGFP, mScarlet) become magnetoresponsive in the presence of an appropriate cofactor (e.g. EGFP-FlavinTag, or an mScarlet/FMN solution). This method works at room-temperature and body-temperature, in vitro, in E. coli and in cultured mammalian cells. The GFP-family magnetoresponse is weak (ΔF/F≈1%), but shows the hallmarks of evolvability. This suggests exciting technological possibilities, both short-term (e.g. lock-in detection, multiplexing) and long-term (e.g. optically-detected MRI, magnetogenetics). We've also discovered weak magnetoresponse from a member of the LOV-domain family. This suggests the possibility that magnetoresponse is a general feature of fluorescent proteins, and not unique to the cryptochrome/photolyase family.
Conference Presentation
© (2024) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Maria Ingaramo, Rebecca Frank Hayward, Julia R. Lazzari-Dean, and Andrew G. York "Magnetic control of GFP-like fluorescent proteins", Proc. SPIE PC12863, Quantum Effects and Measurement Techniques in Biology and Biophotonics, PC128630U (13 March 2024); https://doi.org/10.1117/12.3004017
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KEYWORDS
Fluorescent proteins

Magnetism

In vitro testing

Magnetic resonance imaging

Multiplexing

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