Department of Chemistry and Biochemistry, Ludwig-Maximilian University, 80539 Munich, Germany.
Chemistry. 2010 Jun 18;16(23):6983-92. doi: 10.1002/chem.200903369.
A modified gold surface that allows photoregulated binding of alpha-chymotrypsin has previously been reported. Here the development of this surface is reported, through the synthesis of a series of trifluoromethyl ketones and alpha-keto esters containing the azobenzene group and a surface attachment group as photoswitch inhibitors of alpha-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 alpha-chymotrypsin to a degree that could be modulated by UV/Vis irradiation, showing "slow-tight" enzyme binding as observed for inhibitors in solution.
先前已经有报道称，一种改良的金表面可以实现光调控的糜蛋白酶结合。本研究通过合成一系列含偶氮苯基团和表面连接基团的三氟甲基酮和α-酮酯，报道了这种表面的发展，这些化合物作为糜蛋白酶的光开关抑制剂。所有的化合物都是酶的抑制剂，其活性可以通过光异构化来调节。最好的光开关在光异构化时表现出 IC（50）抑制常数可逆变化>5.3 倍。三氟甲基酮 1 表现出优异的光开关性能，并通过涉及叠氮化物-炔烃环加成的两步程序附着在金表面上。所得的改性表面将α-糜蛋白酶结合到一定程度，可通过 UV/Vis 照射进行调节，表现出与溶液中抑制剂观察到的“慢紧”酶结合。
