The control of enzyme activity has wide applications both in vitro and in vivo. One important strategy of enzyme inhibition is the modification of the catalytic residue of enzyme. We have has successfully developed a strategy to acylate the active sites of serine hydroxyl of serine proteases with a photolabile moiety. The enzymes can be released under light and the activity of enzymes can be fully restored.

New 2-amino cinnamates have been synthesized. The aim for this exploration is to find better inhibition, reactivation and selection to the serine proteases. And by different substitutions on the amino group, we are exploring ways to adjust the process of inhibition and photo activation. In addition, the substitution of the amine group widens the application of this strategy to other general chemical problems.