Photothermally switchable peptide nanostructures towards modulating catalytic hydrolase activity

Enzymes are the most efficient catalysts in nature that possess an impressive range of catalytic activities, albeit limited by stability in adverse conditions. Functional peptides have emerged as alternative robust biocatalysts to mimic complex enzymes. Here, a rational design of minimalistic amyloid-inspired peptides 1-2 is demonstrated, which leads to pathway-driven self-assembly triggered by heat, light and chemical cues to render 1D and 2D nanostructures by the interplay of hydrogen bonding, host-guest interaction and reversible photodimerization. Such in situ transformable peptide nanostructures by means of external cues are envisaged as a catalytic amyloid for the first time to mimic the hydrolase enzyme activity. Michaelis Menten's enzyme kinetic parameters for the hydrolysis rate correlate the external cue-mediated structure-function augmentation with the twisted bundles, 1 TB being the most efficient biocatalyst among all the dimensionally diverse nanostructures. Unlike the natural enzyme, the peptide nanostructures exhibited the robust nature of the hydrolase activity over a broad range of temperature and pH. Finally, the peptide nanostructures are explored as efficient heterogeneous flow catalysts to improve the turnover number for the hydrolase activity. The Aβ42 amyloid-inspired peptide fragment renders pathway-driven self-assembled nanostructures mediated by heat, light and chemical cues. They are envisaged as robust biocatalysts with remarkable variation of the hydrolase catalytic efficiency.