Chinese scientists have made important breakthroughs in the development of protein phosphorylation drug targets
October 12, 2018 Source: Ministry of Science and Technology
Window._bd_share_config={ "common":{ "bdSnsKey":{ },"bdText":"","bdMini":"2","bdMiniList":false,"bdPic":"","bdStyle":" 0","bdSize":"16"},"share":{ }};with(document)0[(getElementsByTagName('head')[0]||body).appendChild(createElement('script')) .src='http://bdimg.share.baidu.com/static/api/js/share.js?v=89860593.js?cdnversion='+~(-new Date()/36e5)];On September 26, Liu Tao, the State Key Laboratory of Natural Medicines and Biomimetic Drugs of Peking University School of Pharmacy, published a paper entitled "Proteomic identification of protein" in the Journal of the American Chemical Society (IF=14.357). Tyrosine phosphatase and substrate interactions in living mammalian cells by genetic encoding of irreversible enzyme inhibitors, using genetic engineering and synthetic biology to genetically engineer synthetic phosphorylase inhibitors by genetic engineering On the proteome encoding human cells, a new technology for finding phosphorylation drug targets has been developed. The research results were supported by national key research and development programs, the National Natural Science Foundation and other projects.
The tyrosine phosphorylation modification of proteins is one of the important post-translational modification methods of proteins, which plays an important role in cell signal transduction, and its regulation abnormality is closely related to the occurrence of diseases. This modification is reversibly regulated in the human body by 90 protein tyrosine kinases (PTK, responsible for the addition of phosphate groups) and 103 protein tyrosine phosphatases (PTP, responsible for the removal of phosphate groups). So far, researchers have extensively studied the role of PTK in the development of related diseases. At present, there are more than 20 kinds of PTK-based drugs in clinical application. For many years, both academic and industrial circles have been the focus of the international pharmaceutical industry. In contrast, although there are individual inhibitors of PTP in the clinical research stage, due to the bottleneck of research technology, the research on the function of most PTP and its relationship with disease is still in its infancy.
In response to this international problem, the Liu Tao team of Peking University used the gene codon extension technology to transform a cell's protein translation machinery to achieve a series of synthetic PTP covalent inhibitors in tissue living cells. Further proteomic analysis, in situ capture of disease-induced protein phosphorylation sites and PTP interactions in living cells provides new ideas for discovering new drug targets.
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