Geurink Paul P, Prely Laurette M, van der Marel Gijs A, Bischoff Rainer, Overkleeft Herman S
Leiden Institute of Chemistry and the Netherlands Proteomics Centre, Leiden University, The Netherlands.
Top Curr Chem. 2012;324:85-113. doi: 10.1007/128_2011_286.
Activity-based protein profiling has come to the fore in recent years as a powerful strategy for studying enzyme activities in their natural surroundings. Substrate analogs that bind covalently and irreversibly to an enzyme active site and that are equipped with an identification or affinity tag can be used to unearth new enzyme activities, to establish whether and at what subcellular location the enzymes are active, and to study the inhibitory effects of small compounds. A specific class of activity-based protein probes includes those that employ a photo-activatable group to create the covalent bond. Such probes are targeted to those enzymes that do not employ a catalytic nucleophile that is part of the polypeptide backbone. An overview of the various photo-activatable groups that are available to chemical biology researchers is presented, with a focus on their (photo)chemistry and their application in various research fields. A number of comparative studies are described in which the efficiency of various photo-activatable groups are compared.
近年来，基于活性的蛋白质谱分析作为一种在自然环境中研究酶活性的强大策略而备受关注。与酶活性位点共价且不可逆结合并带有识别或亲和标签的底物类似物，可用于发掘新的酶活性、确定酶是否以及在何种亚细胞位置具有活性，以及研究小分子化合物的抑制作用。一类特定的基于活性的蛋白质探针包括那些采用光可激活基团来形成共价键的探针。此类探针针对的是那些不使用作为多肽主链一部分的催化亲核试剂的酶。本文概述了化学生物学研究人员可用的各种光可激活基团，重点介绍了它们的（光）化学性质及其在各个研究领域的应用。文中还描述了一些比较研究，其中比较了各种光可激活基团的效率。
