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Magnetically Controlled Fluorescent Proteins Developed for Remote Biosensing

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Researchers have engineered fluorescent proteins that can be remotely dimmed and brightened using magnetic fields. This development aims to create remote-controlled biosensors and therapies that can be activated or deactivated as needed.

Andrew York, a physicist at the Chan Zuckerberg Biohub and co-author of a study published in Nature, stated the goal is to develop a "toolbox of magnetically remote-controlled protein functions." His work also includes a preprint study demonstrating similar proteins in nematode worms.

Discovery of Magnetic Dimming

Two years prior, York and biochemist Maria Ingaramo at Calico Life Sciences identified that green fluorescent protein (GFP) dims when exposed to a weak magnet. To enhance this effect, they engineered a more responsive protein named MagLOV, which can have its fluorescence dimmed by 50% or more in a magnetic field.

Mechanism and Applications

A team led by biophysicists Gabriel Abrahams and Harrison Steel at the University of Oxford investigated MagLOV's magnetic sensitivity. Their experiments revealed that MagLOV's dimming is attributed to a quantum effect where the properties of an electron pair within the protein are altered by a magnetic field. This ‘magnetic resonance effect’ allowed researchers to control the fluorescence brightness in Escherichia coli cells expressing MagLOV using a combination of magnetic fields and radio waves.

Researchers utilized this understanding to locate MagLOV-expressing bacterial cells embedded within a silicon block by applying a varying magnetic field. Steel's team plans to explore if MagLOV-expressing cells can be similarly mapped in living animals. As MagLOV is genetically encoded, it could potentially be used for remote monitoring of various molecular processes, leveraging magnets' ability to penetrate tissues.