Ceria nanoparticles immobilized with self-assembling peptide for biocatalytic applications

Area of Science:

• Biocatalysis
• Nanotechnology
• Materials Science

Background:

• Peptide-based artificial enzymes offer enzyme-like structures and mechanisms but lack reusability in solution.
• Immobilizing self-assembling peptides on nanoparticles enhances local peptide density, promoting cooperative effects and improved catalytic properties.
• Nanoparticle immobilization overcomes limitations of homogeneous peptide catalysts, offering better stability and reusability.

Purpose of the Study:

• To create a stable, reusable heterogeneous artificial enzyme by immobilizing a catalytic peptide onto nanoparticles.
• To investigate the enhanced catalytic activities and potential applications of the immobilized peptide.
• To address the reusability challenges of homogeneous peptide-based artificial enzymes.

Main Methods:

• Immobilization of a branched, self-assembled, nanofibrous catalytic peptide ((C12-SHD)2KK(Alloc)-NH2) onto thiolated ceria nanoparticles.
• Characterization of the resulting heterogeneous catalyst for enhanced catalytic sites and stability.
• Evaluation of the artificial enzyme's mimicked activities (esterase, phosphatase, haloperoxidase) and reusability.

Main Results:

• The immobilized peptide on ceria nanoparticles formed a multifunctional heterogeneous biocatalyst.
• The artificial enzyme exhibited esterase, phosphatase, and haloperoxidase activities.
• Catalytic efficiency remained largely unchanged after multiple uses, demonstrating excellent reusability.

Conclusions:

• A facile method for developing multifunctional heterogeneous biocatalysts using peptide-nanoparticle conjugates was established.
• The developed artificial enzyme overcomes the instability and reusability issues of homogeneous peptide catalysts.
• This approach shows significant potential for diverse industrial applications, including pesticide detection, bone regeneration, and antibiofouling.