Radiofrequency remote control of thermolysin activity
Abstract The majority of biological processes are regulated by enzymes, precise control over specific enzymes could create the potential for controlling cellular processes remotely. We show that the thermophilic enzyme thermolysin can be remotely activated in 17.76 MHz radiofrequency (RF) fields whe...
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Nature Portfolio
2021
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oai:doaj.org-article:2ec73bc33b3443718a0c47ffe94e8fb62021-12-02T17:05:45ZRadiofrequency remote control of thermolysin activity10.1038/s41598-021-85611-w2045-2322https://doaj.org/article/2ec73bc33b3443718a0c47ffe94e8fb62021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-85611-whttps://doaj.org/toc/2045-2322Abstract The majority of biological processes are regulated by enzymes, precise control over specific enzymes could create the potential for controlling cellular processes remotely. We show that the thermophilic enzyme thermolysin can be remotely activated in 17.76 MHz radiofrequency (RF) fields when covalently attached to 6.1 nm gold coated magnetite nanoparticles. Without raising the bulk solution temperature, we observe enzyme activity as if the solution was 16 ± 2 °C warmer in RF fields—an increase in enzymatic rate of 129 ± 8%. Kinetics studies show that the activity increase of the enzyme is consistent with the induced fit of a hot enzyme with cold substrate.Christian B. CollinsRyan A. RiskowskiChristopher J. AckersonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-7 (2021) |
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Medicine R Science Q Christian B. Collins Ryan A. Riskowski Christopher J. Ackerson Radiofrequency remote control of thermolysin activity |
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Abstract The majority of biological processes are regulated by enzymes, precise control over specific enzymes could create the potential for controlling cellular processes remotely. We show that the thermophilic enzyme thermolysin can be remotely activated in 17.76 MHz radiofrequency (RF) fields when covalently attached to 6.1 nm gold coated magnetite nanoparticles. Without raising the bulk solution temperature, we observe enzyme activity as if the solution was 16 ± 2 °C warmer in RF fields—an increase in enzymatic rate of 129 ± 8%. Kinetics studies show that the activity increase of the enzyme is consistent with the induced fit of a hot enzyme with cold substrate. |
format |
article |
author |
Christian B. Collins Ryan A. Riskowski Christopher J. Ackerson |
author_facet |
Christian B. Collins Ryan A. Riskowski Christopher J. Ackerson |
author_sort |
Christian B. Collins |
title |
Radiofrequency remote control of thermolysin activity |
title_short |
Radiofrequency remote control of thermolysin activity |
title_full |
Radiofrequency remote control of thermolysin activity |
title_fullStr |
Radiofrequency remote control of thermolysin activity |
title_full_unstemmed |
Radiofrequency remote control of thermolysin activity |
title_sort |
radiofrequency remote control of thermolysin activity |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/2ec73bc33b3443718a0c47ffe94e8fb6 |
work_keys_str_mv |
AT christianbcollins radiofrequencyremotecontrolofthermolysinactivity AT ryanariskowski radiofrequencyremotecontrolofthermolysinactivity AT christopherjackerson radiofrequencyremotecontrolofthermolysinactivity |
_version_ |
1718381782966992896 |