Lipid Modification of Proteins through Sortase-Catalyzed Transpeptidation

被引:119
作者
Antos, John M. [1 ]
Miller, Gwenn M. [1 ]
Grotenbreg, Gijsbert M. [1 ]
Ploegh, Hidde L. [1 ]
机构
[1] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1021/ja806779e
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:16338 / 16343
页数:6
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