Pearson David, Alexander Nathan, Abell Andrew D
Department of Chemistry, University of Canterbury, Christchurch, New Zealand.
Chemistry. 2008;14(24):7358-65. doi: 10.1002/chem.200800082.
A series of peptidomimetic trifluoromethylketones containing the photoisomerisable azobenzene group have been synthesised, photoisomerised and assayed against the serine protease alpha-chymotrypsin. All are inhibitors of the enzyme and exhibit up to a fivefold increase in activity on UV irradiation. Visible irradiation returns activity to close to that of the original sample. These results suggest the trifluoromethylketone group to be the best electrophilic enzyme binding group for use in photoswitch inhibitors of alpha-chymotrypsin.
一系列含有可光异构化偶氮苯基团的拟肽三氟甲基酮已被合成、进行光异构化，并针对丝氨酸蛋白酶α-胰凝乳蛋白酶进行了测定。所有这些都是该酶的抑制剂，在紫外线照射下活性可提高至五倍。可见光照射后活性恢复到接近原始样品的水平。这些结果表明三氟甲基酮基团是用于α-胰凝乳蛋白酶光开关抑制剂的最佳亲电酶结合基团。
