Work

Lipid Modification of Proteins through Sortase-Catalyzed Transpeptidation

Year: 2008

Type: article

Abstract: 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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja806779e

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

Institution: Whitehead Institute for Biomedical Research

Language: English

Topic: Biochemical and Structural Characterization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: National Cancer Institute, National Institute of Allergy and Infectious Diseases, National Institute of Biomedical Imaging and Bioengineering