Engineering intracellular biomineralization and biosensing by a magnetic protein
Remote measurement and manipulation of biological systems can be achieved using magnetic techniques, but a missing link is the availability of highly magnetic handles on cellular or molecular function. Here we address this need by using high-throughput genetic screening in yeast to select variants o...
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| Format: | Article |
| Language: | en_US |
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Nature Publishing Group
2015
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| Online Access: | http://hdl.handle.net/1721.1/99733 https://orcid.org/0000-0001-6495-5197 https://orcid.org/0000-0002-2834-6359 https://orcid.org/0000-0003-0946-0401 |
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| author | Matsumoto, Yuri Chen, Ritchie Anikeeva, Polina Olegovna Jasanoff, Alan Pradip |
| author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Matsumoto, Yuri Chen, Ritchie Anikeeva, Polina Olegovna Jasanoff, Alan Pradip |
| author_sort | Matsumoto, Yuri |
| collection | MIT |
| description | Remote measurement and manipulation of biological systems can be achieved using magnetic techniques, but a missing link is the availability of highly magnetic handles on cellular or molecular function. Here we address this need by using high-throughput genetic screening in yeast to select variants of the iron storage ferritin (Ft) that display enhanced iron accumulation under physiological conditions. Expression of Ft mutants selected from a library of 10[superscript 7] variants induces threefold greater cellular iron loading than mammalian heavy chain Ft, over fivefold higher contrast in magnetic resonance imaging, and robust retention on magnetic separation columns. Mechanistic studies of mutant Ft proteins indicate that improved magnetism arises in part from increased iron oxide nucleation efficiency. Molecular-level iron loading in engineered Ft enables detection of individual particles inside cells and facilitates creation of Ft-based intracellular magnetic devices. We demonstrate construction of a magnetic sensor actuated by gene expression in yeast. |
| first_indexed | 2024-09-23T12:50:39Z |
| format | Article |
| id | mit-1721.1/99733 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T12:50:39Z |
| publishDate | 2015 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | mit-1721.1/997332022-09-28T10:23:34Z Engineering intracellular biomineralization and biosensing by a magnetic protein Matsumoto, Yuri Chen, Ritchie Anikeeva, Polina Olegovna Jasanoff, Alan Pradip Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. Department of Brain and Cognitive Sciences Massachusetts Institute of Technology. Department of Materials Science and Engineering Massachusetts Institute of Technology. Department of Nuclear Science and Engineering Massachusetts Institute of Technology. Research Laboratory of Electronics Matsumoto, Yuri Chen, Ritchie Anikeeva, Polina Olegovna Jasanoff, Alan Pradip Remote measurement and manipulation of biological systems can be achieved using magnetic techniques, but a missing link is the availability of highly magnetic handles on cellular or molecular function. Here we address this need by using high-throughput genetic screening in yeast to select variants of the iron storage ferritin (Ft) that display enhanced iron accumulation under physiological conditions. Expression of Ft mutants selected from a library of 10[superscript 7] variants induces threefold greater cellular iron loading than mammalian heavy chain Ft, over fivefold higher contrast in magnetic resonance imaging, and robust retention on magnetic separation columns. Mechanistic studies of mutant Ft proteins indicate that improved magnetism arises in part from increased iron oxide nucleation efficiency. Molecular-level iron loading in engineered Ft enables detection of individual particles inside cells and facilitates creation of Ft-based intracellular magnetic devices. We demonstrate construction of a magnetic sensor actuated by gene expression in yeast. National Institutes of Health (U.S.) (Grant DP2-OD002114) National Institutes of Health (U.S.) (Grant R01-NS076462) National Institutes of Health (U.S.) (Grant R01-MH103160) Thomas and Stacey Siebel Foundation (Fellowship) McGovern Institute for Brain Research at MIT (Friends of the McGovern Institute Fellowship) 2015-11-05T18:12:47Z 2015-11-05T18:12:47Z 2015-11 2015-03 Article http://purl.org/eprint/type/JournalArticle 2041-1723 http://hdl.handle.net/1721.1/99733 Matsumoto, Yuri, Ritchie Chen, Polina Anikeeva, and Alan Jasanoff. “Engineering Intracellular Biomineralization and Biosensing by a Magnetic Protein.” Nat Comms 6 (November 2, 2015): 8721. © 2015 Macmillan Publishers Limited https://orcid.org/0000-0001-6495-5197 https://orcid.org/0000-0002-2834-6359 https://orcid.org/0000-0003-0946-0401 en_US http://dx.doi.org/10.1038/ncomms9721 Nature Communications Creative Commons Attribution http://creativecommons.org/licenses/by/4.0/ application/pdf Nature Publishing Group Nature |
| spellingShingle | Matsumoto, Yuri Chen, Ritchie Anikeeva, Polina Olegovna Jasanoff, Alan Pradip Engineering intracellular biomineralization and biosensing by a magnetic protein |
| title | Engineering intracellular biomineralization and biosensing by a magnetic protein |
| title_full | Engineering intracellular biomineralization and biosensing by a magnetic protein |
| title_fullStr | Engineering intracellular biomineralization and biosensing by a magnetic protein |
| title_full_unstemmed | Engineering intracellular biomineralization and biosensing by a magnetic protein |
| title_short | Engineering intracellular biomineralization and biosensing by a magnetic protein |
| title_sort | engineering intracellular biomineralization and biosensing by a magnetic protein |
| url | http://hdl.handle.net/1721.1/99733 https://orcid.org/0000-0001-6495-5197 https://orcid.org/0000-0002-2834-6359 https://orcid.org/0000-0003-0946-0401 |
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