Inhibition of protein breakdown
July 04, 2019 Source: Science and Technology Daily
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)];Technology Daily Tel Aviv, July 2 (Reporter Mao Li) An international team led by scientists at the Israel Institute of Technology discovered how cyclic peptides inhibit cancer and promote protein breakdown, thereby promoting cancer cell growth and reproduction. Researchers believe that the strategies they develop will pave the way for new anti-cancer therapies based on cyclic peptides. The research results are considered to be a milestone in the application of the ubiquitin system, and the related papers are published in the latest issue of Nature and Chemistry.
Israeli and American scientists have previously discovered that ubiquitin (or ubiquitin) can label defective proteins with a "death marker" that decomposes under the action of proteases and thus won the 2004 Nobel Prize in Chemistry. The ubiquitin system is essential for the health of an organism, and disruption of the system can cause various cancers, amyotrophic lateral sclerosis, cystic fibrosis, Parkinson's disease, and other neurodegenerative diseases.
Currently, ubiquitin research plays a key role in understanding and treating cell division in certain types of cancer. The first stage of normal activity of the ubiquitin system is the production of a ubiquitin chain, which then labels the protein to be decomposed. However, when cancer develops in the body, cancer cells know how to operate in the ubiquitin system to maintain their survival and proliferation.
A strategy led by Professor Ashraf Brick, head of the Institute of Polycyclic Peptide Anticancer Research at the Israel Institute of Technology, aims to offset the ability of malignant tumors to function in the ubiquitin system, based on ubiquitin-chain chemical production techniques and large-scale Binding between two libraries of cyclic peptide molecules. In the study, they found how cyclic peptides bind to ubiquitin chains, preventing ubiquitin from labeling cancer-promoting proteins, thereby inhibiting cancer-promoting protein breakdown.
The team said they used the highly uniform ubiquitin chains obtained by chemically synthesized protein technology to screen trillions of molecules in large cyclic peptide libraries and found and confirmed the nascent cyclic peptides that bind tightly to the K48-linked ubiquitin chain. These cyclic peptides protect K48 from the ubiquitin chain from deubiquitinating enzymes and prevent ubiquitin-labeled proteins from being degraded by proteases.
Professor Brick said that the development of ubiquitin system application research and related drug development is very slow. The team believes that a highly synthetic approach with both in vitro protein target generation and cyclic peptide discovery will allow other well-modified targets to be used for drug discovery and to pave the way for the development of new anti-cancer therapies based on cyclic peptides.
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