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Lipid Modification of Proteins through Sortase-Catalyzed Transpeptidation

2008; American Chemical Society; Volume: 130; Issue: 48 Linguagem: Inglês

10.1021/ja806779e

1943-2984

John M. Antos, Gwenn M. Miller, Gijsbert M. Grotenbreg, Hidde L. Ploegh,

Glycosylation and Glycoproteins Research

A general chemoenzymatic method for the site-specific attachment of lipids to protein substrates is described. Sortase A is used to append short lipid-modified oligoglycine peptides to the C terminus of protein substrates bearing a five amino acid sortase A recognition sequence (LPETG). We demonstrate the attachment of a range of hydrophobic modifications in excellent yield (60-90%), including a simple step for removing the sortase enzyme postreaction. Lipoproteins prepared using these procedures were subsequently shown to associate with mammalian cells in a lipid tail-dependent fashion and localized to the plasma membrane and endosomes.