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Chemoenzymatic synthesis of glycosylphosphatidylinositol-anchored glycopeptides.

ABSTRACT: 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.

SUBMITTER: Wu Z 

PROVIDER: S-EPMC3166627 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Chemoenzymatic synthesis of glycosylphosphatidylinositol-anchored glycopeptides.

Wu Zhimeng Z   Guo Xueqing X   Guo Zhongwu Z  

Chemical communications (Cambridge, England) 20100624 31

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. ...[more]

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