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射频远程控制溶菌酶活性。

Radiofrequency remote control of thermolysin activity.

机构信息

Department of Chemistry, Campus Delivery 1872, Colorado State Unviersity, Fort Collins, CO, 80523-1827, USA.

Department of Physics, University of Nebraska - Omaha, Omaha, NE, 68182, USA.

出版信息

Sci Rep. 2021 Mar 16;11(1):6070. doi: 10.1038/s41598-021-85611-w.

DOI:10.1038/s41598-021-85611-w
PMID:33727669
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7971047/
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.

摘要

大多数生物过程都受到酶的调节,对特定酶的精确控制可能为远程控制细胞过程创造潜力。我们表明,当共价附着在 6.1nm 金涂覆磁铁矿纳米颗粒上时,嗜热酶 thermolysin 可以在 17.76MHz 射频 (RF) 场中被远程激活。在不提高溶液的体相温度的情况下,我们观察到酶的活性,就好像溶液在 RF 场中升温了 16±2°C-酶反应速率提高了 129±8%。动力学研究表明,酶活性的增加与冷底物的热酶的诱导契合一致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/ca56b4d18488/41598_2021_85611_Sch1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/5160d95c0685/41598_2021_85611_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/515bb953d936/41598_2021_85611_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/ea683a00a080/41598_2021_85611_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/d43d5c9776e4/41598_2021_85611_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/ca56b4d18488/41598_2021_85611_Sch1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/5160d95c0685/41598_2021_85611_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/515bb953d936/41598_2021_85611_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/ea683a00a080/41598_2021_85611_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/d43d5c9776e4/41598_2021_85611_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5647/7971047/ca56b4d18488/41598_2021_85611_Sch1_HTML.jpg

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本文引用的文献

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交变磁场对酶的激活:生物偶联方法的重要性。
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