Researchers at Peking University reported that they have developed a genetically encoded protein photocrosslinker with a transferable, mass spectrometrically identifiable label. The research was published in the July 27 issue of Nature Communications.
Peng R. Chen, a researcher at the School of Chemistry and Molecular Engineering at Peking University, and Chu Wang, a researcher, are co-authors of the paper.
Proteins function based on their own structure and interactions with other proteins. Therefore, studying the structure and interaction inhibition of proteins is an important direction in life sciences.
Traditional methods for detecting protein interactions, such as yeast two-hybrid, affinity chromatography, and co-immunoprecipitation, have their own limitations. Yeast two-hybrid can reveal direct interactions between proteins, even through large-scale screening to find unknown interactions, but yeast cells may not provide suitable interaction conditions for heterologously expressed proteins of other species. Affinity chromatography and co-immunoprecipitation have relatively low flux, and background binding proteins are sometimes indistinguishable from specific binding proteins, and direct and indirect interactions are often difficult to distinguish. In addition, these three methods are difficult to obtain effective information for transient, weak interactions, such as protein complexes that are loosely changing during signal transduction.
In recent years, scientists have been continually developing techniques for discovering and characterizing the interaction of proteins under physiological conditions, and the chemical and photoaffinity cross-linking strategies have received increasing attention. The conversion of non-covalent interactions between biomolecules into covalent cross-linking enables the capture of weak and transient protein interactions that often occur in nature. Photocrosslinker combined with mass spectrometry is a powerful tool for studying protein interactions in living systems in recent years, but it still has the disadvantages of high false positive discrimination rate and the inability to provide interaction interface information.
In this article, the researchers report that they have developed a genetically encoded photo-affinity and unnatural amino acid that can be used to identify a mass spectrometric label (MS-label) after photocrosslinking and prey protein-bait protein separation. Import into the captured prey protein. This strategy, called IMAPP, enables the direct identification of light-trapping substrate peptides that are difficult to reveal using traditional genetically encoded photocrosslinkers. Using this MS-label, the IMAPP strategy significantly improves the credibility of identifying protein interactions, enabling simultaneous identification of captured peptides and exact cross-linking sites, with the ability to reveal target proteins and map protein interaction interfaces in living systems. Extremely high value.
A team of researchers from the University of Toronto's Lunenfeld-Tanenbaum Research Institute (LTRI) and the Donnelly Center developed a new technology that stitches intracellular DNA barcodes together to search for millions of protein pairs simultaneously. Analyze protein interactions. The results of the study were published in the April 22, 2016 issue of Molecular Systems Biology (a new technology for studying protein interactions).
Scientists at the Scripps Research Institute (TSRI) have developed a powerful new approach to finding candidate drugs that bind to specific proteins. This new approach, published in the June 2016 issue of Nature, is a major advancement that can be applied to a large number of proteins simultaneously, even directly to thousands of different proteins in a natural cellular environment. Some small molecules can be used to determine the function of their target proteins and can serve as a starting complex for drug development. TSRI researchers have confirmed that this technology has found a "ligand" (binding partner protein) for many proteins that were previously thought to be incapable of combining these small molecules (Nature has released a breakthrough protein new technology).
Protein is a natural machine. They supply oxygen to power our muscles, catalyze reactions that help us extract energy from food, and protect against bacterial and viral infections. For decades, scientists have been looking for ways to design new proteins that meet certain medical, research, and industrial-specific uses. Now, researchers at the University of North Carolina School of Medicine have developed a way to generate new proteins by splicing together fragments of existing proteins. The technology, called SEWING, was published in the May 2016 issue of Science (Science publishes breakthrough protein technology).
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