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

Chemical Communications Pub Date: 2021-01-29 DOI: 10.1039/D0CC08309G

Abstract

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.

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