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近年来,发展蛋白质与多肽的化学选择性连接与修饰方法已成为化学生物学的研究热点。这类方法可以在很大程度上弥补基因工程技术无法制备翻译后修饰蛋白与人工改造蛋白的缺陷,得到目前无法通过生物表达的功能蛋白。20世纪90年代末,人们从金黄色葡萄球菌中分离得到转肽酶Sortase A,它能够选择性识别特异性多肽序列LPXTG,并在特定位点切断氨基酸的肽键进而将其与一个新的肽链连接。该特性使Sortase A有望成为一种高效、通用的蛋白质修饰的工具。与传统的化学合成相比,Sortase催化的化学半合成方法,可以较好的解决化学合成蛋白的尺寸问题。本文就近年来Sortase A在蛋白质修饰及合成中的研究进展进行简要综述。
In recent years, the development of chemical and peptide chemistry and selective attachment and modification methods have become the focus of chemical biology. This kind of method can largely compensate for the defect that gene engineering can not prepare post-translationally modified protein and artificial modification protein, and obtain the functional protein which can not be expressed by organisms at present. In the late 1990s, people have isolated the transpeptidase Sortase A from Staphylococcus aureus, which can selectively recognize the specific polypeptide sequence LPXTG and cleave the peptide bond of the amino acid at a specific site to associate it with a new peptide Chain link. This feature makes Sortase A an efficient and versatile protein modification tool. Compared with the traditional chemical synthesis, Sortase catalytic chemical synthesis methods, can be a better solution to the size of chemically synthesized proteins. This review summarizes the research progress of Sortase A in protein modification and synthesis in recent years.