Sugar-assisted ligation of N-linked glycopeptides with broad sequence tolerance at the ligation junction.
A novel method for the synthesis of N-linked glycopeptides using the sugar-assisted ligation strategy from cysteine free peptides is presented. The ligation junction tolerates a variety of amino acids, favoring less hindered amino acids and those with side chains that could serve as a general base in the ligation pathway. Since our approach allows the ligation of difficult junctions, the method could be applied to the synthesis of large peptides by enzymatic removal of the sugar moiety. Alternatively, more complex glycopeptides can be synthesized using glycosyltransferases. Together, this sequence of reactions should be amenable to the synthesis of glycopeptides and glycoproteins and their deglycosylated products.
Brik
Ashraf
A
Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. abrik@bgu.ac.il
Ficht
Simon
S
Yang
Yu-Ying
YY
Bennett
Clay S
CS
Wong
Chi-Huey
CH
D002241:Carbohydrates / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D006020:Glycopeptides / Q000737:chemistry*; D006031:Glycosylation; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D002241:Carbohydrates; D006020:Glycopeptides