Nanozyme Mimics Natural Peroxidase Activity

By doping graphene with nitrogen and boron, scientists in South Korea have create enzyme-like nanomaterials that could be used in bioassays.

AsianScientist (May 16, 2019) – Scientists in South Korea have succeeded in synthesizing a peroxidase-mimicking nanozyme at low cost and with superior catalytic activity. They published their work in ACS Nano.

Enzymes are the main catalysts in our body and are widely used in bioassays. In particular, peroxidase, which oxidizes transparent colorimetric substrates into colored products in the presence of hydrogen peroxide, is the most common enzyme that is used in colorimetric tests.

However, natural enzymes consisting of proteins are costly, unstable when exposed to various temperatures and pH and difficult to synthesize. Researchers have sought to overcome the limitations of natural enzymes by synthesizing artificial enzymes known as nanozymes. However, most nanonzymes are not sufficiently selective in the reactions they catalyze.

In the present study, scientists led by Professor Lee Jinwoo developed a nanozyme that mimics peroxidase and has superior catalytic activity and selectivity toward hydrogen peroxide. They achieved this by doping graphene with nitrogen and boron, which selectively increased the peroxidase-like activity of graphene without inducing any oxidase activity in the nanozyme.

The researchers also showed that the nitrogen and boron co-doped graphene could be used in the the colorimetric detection of acetylcholine, which is an important neurotransmitter in the brain.

“We began to study nanozymes due to their potential to replace existing enzymes. With this study, we have secured core technologies to synthesize nanozymes that have high enzyme activity and are selective as well. We believe that they can be applied to effectively detect acetylcholine for quickly diagnosing Alzheimer’s disease,” said Lee.

The article can be found at: Kim et al. (2019) N- and B-Codoped Graphene: A Strong Candidate To Replace Natural Peroxidase in Sensitive and Selective Bioassays.


Source: Korea Advanced Institute of Science and Technology; Photo: Shutterstock.
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