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 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.

Remote Control of Bovine Catalase Activity with Specific Frequencies of Human and Bovine Catalase with and without bound NADP+

“…Among those studies, some show remarkable increase in enzymatic activity. Many techniques immobilize enzymes on nanoparticles, deactivating and deforming them when exposed to magnetic elds, increasing their activity by about 130% [3,4,5]. iNOS, CAT and Cyt P450 proteins were stimulated by extremely low frequency electromagnetic elds and their activities were changed signi cantly [6].…”

Modulation of α-Chymotrypsin Conjugated to Magnetic Nanoparticles by the Non-Heating Low-Frequency Magnetic Field: Molecular Dynamics, Reaction Kinetics, and Spectroscopy Analysis

“… 13 This approach is different from the radiofrequency magnetic hyperthermia that is well documented elsewhere. 14 − 17 The superparamagnetic MNPs undergo rotational and vibrational motion in the LFMF, which can generate stretching, twisting, and bending forces translated to the macromolecules linked to these nanoparticles, and result in the secondary structure and catalytic activity changes in the conjugated enzyme. 18 , 19 We term this approach magneto–nanomechanical actuation.…”

“…The solution to this problem was proposed using enzymes conjugated to magnetic nanoparticles (MNPs) and demonstrating that enzymes in such conjugates can undergo changes in catalytic activity in the non-heating low-frequency magnetic field (LFMF) . This approach is different from the radiofrequency magnetic hyperthermia that is well documented elsewhere. − The superparamagnetic MNPs undergo rotational and vibrational motion in the LFMF, which can generate stretching, twisting, and bending forces translated to the macromolecules linked to these nanoparticles, and result in the secondary structure and catalytic activity changes in the conjugated enzyme. , We term this approach magneto–nanomechanical actuation. By improving the precision of macromolecule attachment to MNPs using modern synthetic chemical or biological conjugation tools, one can possibly achieve simultaneous actuation and control of the biocatalytic function by the remote magnetic field in billions of enzyme molecules in bulk or at the interfaces.…”