Untitled Document

References

Main Article:

Wang, Z.-G.; Warren, J. D.; Vadim, Y. D.; Xufang, Z.; Iserloh, U.; Visser, M.; Eckhardt,
M.; Seeberger, P. H.; Danishefsky, S. J. Tetrahedron 2006, 62, 4954-4978.

1) Imperiali, B.; O’Connor, S. E. Curr. Opin. Chem. Biol. 1999, 3, 643-649.

A. This article explains how N-linked glycosylation works. In N-linked glycosylation, a polypeptide becomes covalently bonded to a carbohydrate via the amide group attached to the polypeptide. First, the group attached at the anomeric center of the carbohydrate is protonated. In our reaction, an –OH group is protonated by HOBt. The amide group then attacks the anomeric center of the carbohydrate and attaches itself. The protonated –OH group on the anomeric center of the carbohydrate then detaches itself and leaves. The amide group then is deprotonated with a base and the new glycopeptide is formed. In our reaction, the base that is used is DMSO.

Figure 1: A general scheme for a glycosylation reaction.

B. Meyer, B.; Moller, H. Top. Curr.Chem. 2007, 40, 187-251.

This article shows N-linked glycosylations between proteins and sugars, which is type of mechanism used in our reaction.

C. Wu, J. X.; Zhao, X. Y.; Pan, R.; He, R. Q. Int. J. Biol. Macromol 2007, 40, 399-406.

This article discusses glycosylations of isozymes in earthworm proteases.

D. Khajehpour, M.; Dashnau, J. L.; Vanderkool, J. M. Anal. Biochem. 2006, 348, 40-48.

This article uses IR spectroscopy to study glycosylated proteins. These same proteins are involved in the synthesis of our reaction.

2) Arsequell, G.; Valencia, G. Tetrahedron 2000, 10, 3045-3094.

3) Live, D. H.; Wang, Z.-G.; Iserloh, U.; Danishefsky, S. J. Org. Lett. 2001, 3, 851.