Recently, there is an increasing demand to study the protein post-translational modification (PTM) in understanding the increase in complexity from the level of the genome to the proteome. The PTM proteins isolated from the natural sources or obtained from recombinant DNA approaches are characterized by the heterogeneity or the incorrect modification structure, which challenges the following biological studies. In this regard, chemical synthesis of proteins will make important contribution to the production of homogeneous PTM proteins with the high homogeneity and the defined structure. In addition, the chemical synthesis will allow for the generation of new bio-macromolecules with altered structures, including the incorporation of unnatural elements, to create new functions. Our laboratory has a long-standing interest in the study of the protein post-translational glycosylation. At the intial stage, we aim to develop chemical methods to enable us to access the synthetic and homogenous glycoproteins which are homogeneous and of a defined structure. Over the past years, we have established a chemoselective peptide ligation, Serine/Threonine Ligation (STL), enabling the synthesis of biologically active proteins. In addition, we are also engaged in the development of new methods and strategies enabling complex glycan synthesis. references: 1) Peng, P.; Liu, H.; Gong, J.; Nicholls, J. M.; Li, X.* Chem. Sci. 2014, 5, 3634. 2) Lee, C. L.; Li, X.* Curr. Opin. Chem. Biol. 2014, 22, 108-114 3) Zhang, Y.; Xu, C.; Lam, H. Y.; Lee, C. L; Li, X.* Proc. Natl. Acad. Sci. USA, 2013, 110, 6657. 4) Lam, H. Y.; Zhang, Y.; Liu, H.; Xu, J.; Wong, C. T.; Xu, C.; Li, X.* J. Am. Chem. Soc. 2013, 135, 6272. 5) Wong, C. T. T.; Lam, H. Y.; Song, T.; Chen, G.*; Li, X.* Angew. Chem. Int. Ed. 2013, 52, 10212.

New tools in glycoprotein chemical synthesis

249th National Meeting (2015)

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