Related Experiment Video
Updated: May 18, 2026
11:20
An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation
Published on: August 30, 2017
Nanoparticle-mediated remote control of enzymatic activity
Leslie D Knecht1, Nur Ali, Yinan Wei
1Department of Chemistry, University of Miami, Miami, Florida 33136, USA.
ACS Nano
|September 20, 2012
Summary
Iron oxide nanoparticles in hydrogels remotely activate enzymes using magnetic fields. This novel approach enhances enzyme activity more efficiently than external heating, enabling new biomedical applications.
Area of Science:
- Biomedical Engineering
- Materials Science
- Nanotechnology
Background:
- Nanomaterials offer tunable, remotely controlled platforms for biomedical applications like drug delivery and hyperthermia cancer treatment.
- Unique nanoscale properties enable remote stimuli to activate secondary systems.
- Iron oxide nanoparticles (Fe3O4) and enzymes can be combined in hydrogels for advanced functionalities.
Purpose of the Study:
- To develop a nanocomposite hydrogel system for remote enzyme activation.
- To investigate the efficiency of magnetic field-induced heating for enzyme activation.
- To explore the potential of this system for biomedical and environmental applications.
Main Methods:
- Encapsulating iron oxide nanoparticles and a model dehalogenase enzyme (L-2-HAD(ST)) within a polyacrylamide hydrogel network.
- Exposing the nanocomposite hydrogel to an alternating magnetic field (AMF) to induce localized heating.
- Comparing enzymatic activity in AMF-heated hydrogels versus externally heated hydrogels (water bath).
Main Results:
- Alternating magnetic field (AMF) exposure led to enhanced system heating.
- The nanocomposite hydrogel showed a 2-fold increase in enzymatic activity compared to external heating.
- Internal nanoparticle heating via AMF was more efficient than diffusion-limited external heating.
Conclusions:
- Remote activation of enzymes is achievable using magnetic nanoparticles embedded in hydrogels.
- Internal heating via AMF is a more efficient method for enzyme activation than external heating.
- This technology holds promise for remote actuation of enzymes in biomedical and environmental fields.
Related Concept Videos
01:00Enzyme-linked Receptors
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
02:34Enzymes
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
01:19Enzyme Kinetics
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
01:30Enzyme Inhibition
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
01:08Allosteric Regulation
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...