Protein-stabilized Ir nanoparticles with usual charge-selective peroxidase properties

Area of Science:

• Nanotechnology
• Biochemistry
• Catalysis

Background:

• Selective removal of organic compounds is challenging in separation processes.
• Protein-stabilized nanoparticles offer unique catalytic properties.

Purpose of the Study:

• To prepare and characterize bovine serum albumin (BSA)-stabilized iridium nanoparticles (IrNPs).
• To investigate the selective catalytic degradation of cationic compounds and amino acids by BSA-IrNPs.
• To evaluate the reusability and potential applications of the synthesized nanozyme.

Main Methods:

• One-step precipitation method for BSA-IrNP synthesis.
• Comprehensive characterization using TEM, XRD, XPS, UV-vis, FT-IR, fluorescence, and circular dichroism.
• Assessing peroxidase-like activity and selective catalysis of cationic compounds and amino acids.

Main Results:

• BSA-IrNPs with an average diameter of 3.6 nm were successfully synthesized.
• The nanozyme demonstrated high peroxidase-like activity and selective catalysis of cationic compounds via H2O2.
• Degradation of amino acids was controllable by pH adjustment, attributed to electrostatic adsorption.
• Excellent reusability was observed through simple recycling methods.

Conclusions:

• BSA-IrNPs function as effective nanozymes with high selectivity for cationic compounds and amino acids.
• The anchoring effect between BSA and amidogen-containing molecules contributes to catalytic selectivity.
• The nanozyme's reusability and selectivity make it promising for applications in complex matrices.