Progress in the analysis of protein post-translational lipid modification

Recently, researchers from the School of Chemistry of Central China Normal University have made significant progress in the research of a new method for mass spectrometry analysis of post-translational lipid modification of proteins. Related research results have been published in the "Nature-Experiment Manual", a sub-journal of the internationally renowned academic journal Nature (Nature Protocols) magazine.

Professor Zhong Hongying of the School of Chemistry of Central China Normal University is the corresponding author of this article. His main research areas are engaged in the research of biological / organic mass spectrometry methods, including new MALDI / ESI technology, mass spectrometry imaging analysis technology, spectrogram analysis method, biological information analysis method of massive mass spectrometry data, and pesticide protein chemistry and related chemical biology issues In particular, the role of lipid groups and post-translational lipid modification of proteins in physiological activities such as signal transduction, protein transport, and membrane anchoring, research on new pesticide targets with high safety, and development of pesticide residue analysis methods and safety evaluation methods.

After the ribosome is translated and synthesized, the protein must be covalently bound with specific small organic molecules (such as phosphorylation, glycosylation, acetylation, lipidation, etc.) to be converted into a protein with a specific function. The process is called protein post-translational modification. The study found that protein lipid modification mainly occurs on membrane proteins and membrane-related proteins. The combination of different types of fatty acids and proteins directly affects the affinity of proteins and different micro-regions of the membrane, and affects the protein between organelles with different membrane structures. Transport is directly involved in regulating cell signal transduction, intracellular protein localization and other physiological activities. However, due to the lack of effective analysis methods, the study of protein lipid modification started late, and its mechanism and function are still unclear.

The main difficulties faced by the analysis of membrane proteins and their post-translational lipid modification include low solubility, low abundance, and the coexistence of multiple modifications. The combination of strong hydrophobic long-chain fatty acids and low-solubility membrane proteins makes them more difficult to dissolve in water, and there are no groups for affinity enrichment, plus a variety of lipid modifications and other modifications such as phosphorylation modifications, sugar groups The coexistence of chemical modification, etc. makes it difficult to carry out accurate qualitative, quantitative and localization analysis. Since lipid modification activation and deactivation states are directly related to their biological functions, there is an urgent need to establish accurate and sensitive analytical methods to detect lipid migration and changes in cells or tissues. At present, there are two methods available for selection: ABE method and CR method, but both methods can only perform qualitative and quantitative analysis of lipid-modified proteins, and cannot determine fatty acids covalently bound to proteins.

In the new study, Zhong Hongying's research group developed a new mass spectrometry method for protein post-translational lipid modification, iFAT method. IFAT overcomes the deficiencies of the above two methods of ABE and CR, and by establishing a protein fluorescent staining method, The structure identification of lipids and quantitative determination of lipid changes were successfully achieved. The establishment of the iFAT method provides a useful research tool for further research on the regulatory network of lipid-modified proteins, discovery of new drug targets, and understanding of the occurrence and development of major human diseases.

Nature Protocols is a sub-journal of the internationally renowned academic journal Nature. The paper was supported by the Ministry of Education's Innovation Team Program (No .: IRT0953), Hubei Provincial Natural Science Foundation Key Project (No .: 2009CDA001), etc.

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