Lipid Modification of Proteins through Sortase-Catalyzed Transpeptidation | Zendy

John M. Antos | Zendy; Gwenn M. Miller | Zendy; Gijsbert M. Grotenbreg | Zendy; Hidde L. Ploegh | Zendy

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Lipid Modification of Proteins through Sortase-Catalyzed Transpeptidation

Author(s) -

John M. Antos,

Gwenn M. Miller,

Gijsbert M. Grotenbreg,

Hidde L. Ploegh

Publication year - 2008

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja806779e

Subject(s) - chemistry , sortase a , sortase , biochemistry , endosome , enzyme , vesicle , amino acid , peptide sequence , membrane , bacterial protein , receptor , gene

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.

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