fumaramide and maleimide

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.

Topics: Amides; Biomimetic Materials; Catalysis; Catalytic Domain; Esterases; Maleimides; Models, Molecular; Peptidomimetics; Photochemical Processes; Protein Folding; Stereoisomerism; Structure-Activity Relationship