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SPPS method for Post-translational modification protein synthesis
Jun 11 , 2020

Proteins play an important physiological role in life. Post-translational modifications (acylation, phosphorylation, ubiquitination, etc.) make proteins more complex and versatile. In order to conduct biophysical research on it, it is necessary to obtain a sufficient quantity of homogeneous samples. The methods of biological extraction and recombinant expression have some limitations in obtaining some functional proteins, especially post-translational modification proteins and circular proteins. Although the development of genetic incorporation of unnatural amino acid solves some key issues, the limitations of the number of unnatural amino acids that can be embedded, the limitations of sites, and the limitations of low yields make this method also have certain problem. Protein chemical synthesis technology can design and synthesize proteins on the atomic scale and obtain some important functional proteins through effective means.


After decades of development, the protein chemical synthesis has undergone qualitative changes. The solid-phase peptide synthesis technology developed by Professor Merrifield simplifies the operation steps and improves the synthesis efficiency. The native chemical ligation method developed by Professor Kent has made it possible to obtain longer and complex proteins. The development of various methods including auxiliary group and peptide hydrazides have broadened the scope of application of protein chemistry for protein synthesis. From the synthesis of the first short peptides to the synthesis of various complex post-translational modification proteins, protein chemical synthesis has become a powerful tool in

chemical biology research.


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