L-亮氨酰对硝基苯胺是多种氨肽酶家族成员活性测试的底物,但其合成工艺鲜有文献报道。经过实验方法研究,以低毒的三光气作为关键试剂,替代文献报道的光气。并在此基础上对反应溶剂、反应温度和三光气的用量等因素进行了考察,优化了反应条件。目标化合物结构通过熔点和核磁共振等手段进行了确证。
As the substrate of various aminopeptidases,L-leucine-p-nitroanilide is widely used for the assay of these enzymes activity.However,very few literatures reported the synthetic methods of this reagent.In this works,the new synthetic method was developed by using the low toxic reagent,triphosgene,to replace the traditional phosgene.Then,this synthetic method was studied on the optimal solvents,temperature,and the ratio between leucine and triphosgene.The structure of the target compound was confirmed according to its melting point and NMR,etc.