期刊
BIOORGANIC CHEMISTRY
卷 76, 期 -, 页码 380-385出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2017.11.018
关键词
WDR5; Biotin; Small-molecule probe; Molecular docking; Chemoprecipitation
资金
- Project Program of State Key Laboratory of Natural Medicines, China Pharmaceutical University [SKLNMZZCX201611]
- National Natural Science Foundation of China [81230078, 81573346, 81502915]
- National Major Science and Technology Project of China [2013ZX09402102-001-005, 2014ZX09507002-005-015]
- Specialized Research Fund for the Doctoral Program of Higher Education [20130096110002]
- Priority Academic Program Development of Jiangsu Higher Education Institutions
WDR5, a subunit of the SET/MLL complex, plays critical roles in various biological progresses and are abnormally expressed in many cancers. Here we report the design, synthesis, and biochemical characterization of a new chemical tool to capture WDR5 protein. The probe is a biotinylated version of compound 30 that is a potent WDR5 inhibitor we previously reported. Importantly, the probe displayed high affinity to WDR5 protein in vitro binding potency and showed the ability in specifically and real time monitoring WDR5 protein. Further, the biotinylated tag of the probe enabled selectively chemoprecipitation of WDR5 from whole cell lysates of MV4-11. This probe provided a new approach to identify the overexpressed WDR5 protein in different cancer cells and applications to proteomic analysis of WDR5 and WDR5-binding partners. (C) 2017 Published by Elsevier Inc.
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