Sortase-catalyzed peptide-glycosylphosphatidylinositol analogue ligation.
It is demonstrated that sortase A (SrtA) can catalyze efficient coupling of peptides to GPI analogues with a glycine residue attached to the phosphoethanolamine moiety at the nonreducing end to form GPI-linked peptides. This represents the first chemoenzymatic synthesis of GPI-peptide conjugates and is a proof-of-concept for the potential application of SrtA to the synthesis of more complex GPI-anchored peptides/glycopeptides and GPI-anchored proteins/glycoproteins.
Guo
Xueqing
X
Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, USA.
Wang
Qianli
Q
Swarts
Benjamin M
BM
Guo
Zhongwu
Z
D019881:Aminoacyltransferases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D055162:Biocatalysis; D002236:Carbohydrate Conformation; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D017261:Glycosylphosphatidylinositols / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*
D001426:Bacterial Proteins; D017261:Glycosylphosphatidylinositols; D010455:Peptides; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases