Journal article icon

Journal article

Quantum spin resonance in engineered proteins for multimodal sensing

Abstract:
Sensing technologies that exploit quantum phenomena for measurement are finding increasing applications across materials, physical and biological sciences1, 2, 3, 4, 5, 6–7. Until recently, biological candidates for quantum sensors were limited to in vitro systems, had poor sensitivity and were prone to light-induced degradation. These limitations impeded practical biotechnological applications, and high-throughput study that would facilitate their engineering and optimization. We recently developed a class of magneto-sensitive fluorescent proteins including MagLOV, which overcomes many of these challenges8. Here we show that through directed evolution, it is possible to engineer these proteins to alter the properties of their response to magnetic fields and radio frequencies. We find that MagLOV exhibits optically detected magnetic resonance in living bacterial cells at room temperature, at sufficiently high signal-to-noise for single-cell detection. These effects are explained through the radical-pair mechanism, which involves the protein backbone and a bound flavin cofactor. Using optically detected magnetic resonance and fluorescence magnetic-field effects, we explore a range of applications, including spatial localization of fluorescence signals using gradient fields (that is, magnetic resonance imaging using a genetically encoded probe), sensing of the molecular microenvironment, multiplexing of bio-imaging and lock-in detection, mitigating typical biological imaging challenges such as light scattering and autofluorescence. Taken together, our results represent a suite of sensing modalities for engineered biological systems, based on and designed around understanding the quantum-mechanical properties of magneto-sensitive fluorescent proteins.
Publication status:
Published
Peer review status:
Peer reviewed

Actions

Access Document

Files:
Publisher copy:
10.1038/s41586-025-09971-3

Authors

More by this author
Institution:
University of Oxford
Role:
Author
ORCID:
0000-0002-2360-7150
More by this author
Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
ORCID:
0000-0002-9304-2773


Publisher:
Nature Research
Journal:
Nature More from this journal
Pages:
1-8
Publication date:
2026-01-21
DOI:
EISSN:
1476-4687
ISSN:
0028-0836


Language:
English
Keywords:
Pubs id:
2363909
UUID:
uuid_a084d3bb-2648-4510-8081-ce2d5051482a
Local pid:
pubs:2363909
Source identifiers:
W7125182252
Deposit date:
2026-01-27
ARK identifier:
This ORA record was generated from metadata provided by an external service. It has not been edited by the ORA Team.

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP