Photothermally switchable peptide nanostructures towards modulating catalytic hydrolase activity

Area of Science:

• Biocatalysis
• Materials Science
• Biotechnology

Background:

• Enzymes are nature's efficient catalysts but often lack stability in harsh conditions.
• Functional peptides offer a robust alternative to mimic enzyme catalytic activities.
• Amyloid-inspired peptides present a designable platform for creating novel biocatalysts.

Purpose of the Study:

• To rationally design minimalistic amyloid-inspired peptides that self-assemble into nanostructures.
• To investigate the in situ transformability of these peptide nanostructures using external cues (heat, light, chemical).
• To explore the potential of these peptide nanostructures as robust hydrolase enzyme mimics.

Main Methods:

• Rational design of amyloid-inspired peptides (1-2).
• Triggered self-assembly into 1D and 2D nanostructures via hydrogen bonding, host-guest interactions, and reversible photodimerization.
• Characterization of nanostructure formation and catalytic activity.
• Enzyme kinetic analysis (Michaelis Menten) to correlate structure and function.
• Assessment of hydrolase activity under varying temperature and pH conditions.
• Exploration as heterogeneous flow catalysts.

Main Results:

• Demonstrated rational design of self-assembling amyloid-inspired peptides.
• Achieved pathway-driven in situ transformation of peptide nanostructures using external cues.
• Identified twisted bundles (1_TB) as the most efficient biocatalyst among diverse nanostructures.
• Peptide nanostructures exhibited robust hydrolase activity across a wide range of temperatures and pH.
• Successfully employed peptide nanostructures as heterogeneous flow catalysts, enhancing turnover numbers.

Conclusions:

• Minimalistic amyloid-inspired peptides can be rationally designed for triggered self-assembly into catalytically active nanostructures.
• These peptide nanostructures serve as robust, artificial hydrolase mimics with tunable activity based on structural transformations.
• The developed peptide nanostructures show promise as efficient heterogeneous flow catalysts for improved biocatalytic applications.