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- Title
Enzymatic Cell‐Surface Decoration with Proteins using Amphiphilic Lipid‐Fused Peptide Substrates.
- Authors
Takahara, Mari; Wakabayashi, Rie; Fujimoto, Naoki; Minamihata, Kosuke; Goto, Masahiro; Kamiya, Noriho
- Abstract
Lipid modification of proteins plays a significant role in the activation of cellular signals such as proliferation. Thus, the demand for lipidated proteins is rising. However, getting a high yield and purity of lipidated proteins has been challenging. We developed a strategy for modifying proteins with a wide variety of synthetic lipids using microbial transglutaminase (MTG), which catalyzes the cross‐linking reaction between a specific glutamine (Q) in a protein and lysine (K) in the lipid‐fused peptide. The synthesized lipid‐G3S‐MRHKGS lipid (lipid: fatty acids, tocopherol, lithocholic acid, cholesterol) was successfully conjugated to a protein fused with LLQG (Q‐tagged protein) by an MTG reaction, yielding >90 % conversion of the Q‐tagged protein in a lipidated form. The purified lipid–protein conjugates were used for labeling the cell membrane in vitro, resulting in best‐anchoring ability of cholesterol modification. Furthermore, in situ cell‐surface decoration with the protein was established in a simple manner: subjection of cells to a mixture of cholesterol‐fused peptides, Q‐tagged proteins and MTG.
- Subjects
TRANSGLUTAMINASES; PROTEINS; MICROBIAL lipids; POST-translational modification; CELL proliferation; CELL membranes
- Publication
Chemistry - A European Journal, 2019, Vol 25, Issue 30, p7315
- ISSN
0947-6539
- Publication type
Article
- DOI
10.1002/chem.201900370