Racemic peptide assembly boosts biocatalysis

Area of Science:

• Biochemistry and Materials Science
• Enzyme catalysis and nanotechnology

Background:

• Minimalistic peptides can be designed as functional biomaterials.
• Histidine is a key residue for catalytic activity in many enzymes.
• Self-assembly of peptides into nanostructures can create novel catalytic environments.

Purpose of the Study:

• To investigate the impact of racemic assembly of heterochiral tripeptides on biocatalytic activity.
• To explore the role of histidine and diphenylalanine motifs in peptide self-assembly and gelation.
• To provide insights for designing advanced green biocatalysts.

Main Methods:

• Synthesis of minimalistic heterochiral tripeptides.
• Characterization of self-assembled nanostructures using techniques like electron microscopy.
• Assay of ester hydrolysis activity of the self-assembled peptide gels.
• Analysis of the influence of amino acid sequence on catalytic performance.

Main Results:

• Racemic assembly of specific tripeptides significantly boosted ester hydrolysis activity compared to non-assembled or homochiral counterparts.
• The diphenylalanine motif successfully directed self-assembly into anisotropic nanostructures, forming stable gels.
• Histidine residues within the assembled structures remained catalytically active, facilitating the hydrolysis reaction.

Conclusions:

• Minimalistic heterochiral tripeptides can be rationally designed for enhanced biocatalysis through self-assembly.
• Self-assembled peptide nanostructures offer a promising platform for developing efficient and sustainable biocatalysts.
• This work highlights the potential of bioinspired materials in green chemistry applications.