Light-mediated control of activity in a photosensitive foldamer that mimics an esterase

We report a catalytic foldamer in which a fumaramide chromophore links a Ser residue to a helical domain that contains within its sequence the residues His and Asp. Photoisomerization of the fumaramide chromophore (with E geometry) to the corresponding maleamide (with Z geometry) brings together a 'catalytic triad' of Ser, His, and Asp, triggering esterase activity that is absent in the fumaramide isomer. The fumaramide/maleamide linker thus acts as a light-sensitive switchable cofactor for activation of catalytic activity in short foldamers.

Automated summary

This study presents a catalytic foldamer containing a fumaramide chromophore that acts as a light-sensitive switchable cofactor, triggering esterase activity when undergoing photoisomerization. The fumaramide/maleamide linker serves as a 'catalytic triad' bringing together Ser, His, and Asp residues for activation of catalytic activity in short foldamers.