Chemoenzymatic synthesis of glycosylphosphatidylinositol-anchored glycopeptides.
MUC1 glycopeptide was efficiently coupled to glycosylphosphatidylinositol (GPI) derivatives by sortase A (SrtA), verifying that SrtA can accept sterically hindered glycopeptide as substrate for ligation with GPIs. This work has established a practical method for the chemoenzymatic synthesis of GPI-linked glycopeptides.
Wu
Zhimeng
Z
Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48202, USA.
Guo
Xueqing
X
Guo
Zhongwu
Z
D000595:Amino Acid Sequence; D019881:Aminoacyltransferases / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D055162:Biocatalysis; D002240:Carbohydrate Sequence; D003546:Cysteine Endopeptidases / Q000378:metabolism; D006020:Glycopeptides / Q000096:biosynthesis* / Q000737:chemistry; D017261:Glycosylphosphatidylinositols / Q000737:chemistry*; D008969:Molecular Sequence Data; D018396:Mucin-1 / Q000737:chemistry
D001426:Bacterial Proteins; D006020:Glycopeptides; D017261:Glycosylphosphatidylinositols; D018396:Mucin-1; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases