Histidine Containing Minimalistic-Peptide-Based Nanostructured Hydrogel for Multiple Enzyme-Mimicking Catalytic...

Area of Science:

• Biomaterials Science
• Catalysis
• Supramolecular Chemistry

Background:

• Enzymes offer exceptional catalytic activity but suffer from poor stability and high production costs.
• Peptide hydrogels present a promising alternative, mimicking enzyme structure and function with enhanced reusability and separation.

Purpose of the Study:

• To design and synthesize a minimalistic peptide hydrogel capable of mimicking enzyme catalytic activity.
• To investigate the gelation and substrate binding mechanisms of the peptide hydrogel.
• To demonstrate the hydrogel's versatility in mimicking metalloenzymes for various catalytic applications.

Main Methods:

• Conception and synthesis of a minimalistic dipeptide hydrogel.
• Molecular dynamics simulations to elucidate gelation and substrate binding.
• Incorporation of metal ion cofactors (Zn²⁺ and Cu²⁺) to mimic metalloenzymes.

Main Results:

• The peptide hydrogel exhibited excellent hydrolase mimicking aptitude.
• The peptide/Zn²⁺ hydrogel effectively catalyzed CO₂ hydrolysis, mimicking carbonic anhydrase.
• The peptide/Cu²⁺ hydrogel catalyzed the oxidation of phenolic compounds and catecholamines, mimicking laccase.

Conclusions:

• A single peptide hydrogel system demonstrates versatile catalytic capabilities by mimicking various enzyme active sites.
• This approach offers a stable, reusable, and easily separable alternative to native enzymes.
• Potential applications span the chemical industry, environmental remediation, and biomedical research.