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  English.dicp.cas.cn    Posted:2016-07-05
Chemical proteomics-quantitative analysis and mechanism study of targets for bioactive molecules

Time:9:30 am, July. 5th of 2016

Location:Academic Report Hall of Department of Biotechnology

Reporter:Prof. Chu Wang, College of Chemistry and Molecular Engineering of Peking University; Synthetic and Functional Biomolecules Center of Peking University; Peking-Tsinghua center for life sciences. He obtained his bachelor degree from department of biological chemistry, university of science and technology of China in 2001 and Ph. D degree from department of biological chemistry, university of Washington in 2007. After that, he carried out postdoctoral research in department of biological chemistry, university of Washington from 2007-2008 and Department of Chemical Physiology, The Scripps Research Institute from 2009-2013. From 2014 until now, he worked in Peking University. His research focused on the development and application of multi-disciplinary tools in chemoproteomics, biochemistry, bioinformatics and computational structure biology to uncover proteome-scale functional sites and targets that are selectively modified by endogenous small biomolecules or exogeneous chemical medicine and investigate the influences of these modification on the structure and function of proteins as well as the metabolism and signaling pathways in cells. He has been honored the NIH K99/R00 Pathway to Independence Postdocotral Award, Baylor scholar award. In recent years, he published a series of publication in famous scientific journals such as Nature Methods, Nature, Nature Chemical Biology and Protein Science.


In recent years, along with the development of analytical chemistry, pharmaceutical chemistry and synthetic chemistry, many small chemical molecules with biological activities including natural products, synthetic compounds, endogenous metabolites and exogenous drug precursor were screened, discovered, separated and synthesize. However, the functional mechanism of these bioactive compounds still need to be further investigated, which is one of the hot spots in chemical biology. In this report, I will introduce a series of activity-based protein profiling technologies based on molecular activity probes, which can be used to quantitatively analyze the target of bioactive molecules in cell proteome at large scale and build a solid foundation for the subsequent functional experiment and mechanism study at molecular level. My report is mainly composed of two parts: (1) identified more than 1000 amino acid sited sensitive to the electrophilic aldehyde modification produced by endogenous metabolism in cells and further discovered a novel functional cysteine site in protein kinase which is selectively modified under oxidative stress and results in the change of kinase signaling pathway in cells. (2) identified the target proteins of bioactive ingredient of Chinese medicine in cells using chemical proteomics techniques and investigated the mechanism of it to reduce the fat accumulation at molecule level.

Contact:Prof. Lihua Zhang of group 1810(9720)




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