Design and synthesis of a novel photoaffinity probe for labelling EGF receptor tyrosine kinases. (1st January 2017)

• Record Type: Journal Article
• Authors: Zheng, You-Guang; Wu, Xiao-Qing; Su, Jun; Jiang, Ping; Xu, Liang; Gao, Jian; Cai, Bin; Ji, Min
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 32:Number 1(2017)
• Page Start: 954
• Page End: 959
• Publication Date: 2017-01-01
• Subjects: Epidermal growth factor receptor -- activity-based protein profiling -- photoaffinity probe; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.1080/14756366.2017.1344979
• Languages: English
• ISSNs: 1475-6366

Abstract

Abstract: The epidermal growth factor receptor (EGFR) and HER2 are two important tyrosine kinases that play crucial roles in signal transduction pathways that regulate numerous cellular functions including proliferation, differentiation, migration, and angiogenesis. In the past 20 years, many proteomic methods have emerged as powerful methods to evaluate proteins in biological processes and human disease states. Among them, activity-based protein profiling (ABPP) is one useful approach for the functional analysis of proteins. In this study, a novel photoaffinity probe11 was designed and synthesised to assess the target profiling of the reactive group in the photoaffinity probe11 . Biological evaluation was performed, and the results showed that the novel photoaffinity probe binds to EGFR and HER2 proteins and it hits targets by the reactive group. Graphical Abstract: