Nanozymes with Modulable Inhibition Transfer Pathways for Thiol and Cell Identification

Area of Science:

• Materials Science
• Nanotechnology
• Biochemistry

Background:

• Nanozyme-based inhibition reactions require clearer mechanisms and site studies.
• Advanced nanozymes are needed to understand inhibition effects at the atomic level.

Purpose of the Study:

• To develop novel nanozymes with tunable inhibition properties for mechanistic studies.
• To investigate the role of specific catalytic and binding sites in nanozyme activity.
• To create a sensor array for detecting cancer cells and thiols.

Main Methods:

• Synthesized nanozymes with single Cu-N catalytic sites and B-O binding sites on a porous nitrogen-doped carbon substrate (B6/CuSA).
• Investigated electron redistribution and its effect on peroxidase-like activity.
• Studied cysteine binding and inhibition mechanisms (competitive and noncompetitive).
• Developed a multichannel sensor array for cell and thiol detection.

Main Results:

• B6/CuSA exhibited enhanced peroxidase-like activity compared to CuSA due to B-O site incorporation.
• CuSA showed competitive inhibition of cysteine via coordination bonds (Ki = 0.048 mM).
• B6/CuSA demonstrated mixed inhibition of cysteine with competitive (Ki = 0.054 mM) and noncompetitive (Ki = 0.71 mM) interactions.
• The sensor array successfully detected various cancer cells, normal cells, and thiols.

Conclusions:

• The developed nanozymes provide atomic-level control over inhibition transfer.
• The study elucidates the inhibition mechanisms of nanozymes with specific catalytic and binding sites.
• This work offers a framework for evaluating thiols, discriminating cells, and predicting diseases.