1240365-01-8Relevant articles and documents
Structural optimization of photoswitch ligands for surface attachment of α-chymotrypsin and regulation of its surface binding
Pearson, David,Abell, Andrew D.
supporting information; experimental part, p. 6983 - 6992 (2010/11/19)
A modified gold surface that allows photoregulated binding of a-chymotrypsin has previously been reported. Here the development of this surface is reported, through the synthesis of a series of trifluoromethyl ketones and a-keto esters containing the azobenzene group and a surface attachment group as photoswitch inhibitors of a-chymotrypsin. All of the compounds are inhibitors of the enzyme, with activity that can be modulated by photoisomerization. The best photoswitch shows a reversible change in IC 50 inhibition constant of >5.3 times on photoisomerization. The trifluoromethyl ketone 1 exhibited excellent photoswitching and was attached to a gold surface in a two-step procedure involving an azide-alkyne cycloaddition. The resulting modified surface bound α-chymotrypsin to a degree that could be modulated by UV/Vis irradiation, showing "slow-tight" enzyme binding as observed for inhibitors in solution.
