A site-specific branching poly-glutamate tag mediates intracellular protein delivery by cationic lipids

Intracellular protein delivery is of significance for cellular protein analysis and therapeutic development, but remains challenging technically. Herein, we report a general and highly potent strategy for intracellular protein delivery based on commercially available cationic lipids. In this strateg...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2018-09, Vol.503 (2), p.671-676
Main Authors: Huang, Si-Qi, Han, Bei-Bei, Li, Yan-Mei, Chen, Yong-Xiang
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
A549 Cells
Amino Acid Sequence
Cationic lipid
Cations - chemistry
ELECTROSTATICS
Glutamic Acid - analogs & derivatives
HeLa Cells
Humans
Intracellular protein delivery
LIPIDS
Lipids - chemistry
LIPOSOMES
Liposomes - chemistry
Negatively charged peptide tag
PEPTIDES
Peptides - chemistry
Protein modification
Proteins - administration & dosage
Proteins - chemistry
Static Electricity
Transfection
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Summary:Intracellular protein delivery is of significance for cellular protein analysis and therapeutic development, but remains challenging technically. Herein, we report a general and highly potent strategy for intracellular protein delivery based on commercially available cationic lipids. In this strategy, a designed double branching poly-glutamate tag is site-specifically attached onto the C-terminal of protein cargos via expressed protein ligation (EPL), which mediates the entrapment of proteins into cationic liposomes driven by electrostatic interaction. The resultant protein-lipid complexes can enter into cytosol with a high efficiency even at the low protein concentration while maintaining protein's biological activity. •We reported a highly potent strategy for intracellular protein delivery.•A branching poly-E tag mediated the entrapment of proteins into liposomes.•The resultant protein-lipid complexes entered into cytosol with a high efficiency.•The strategy maintained protein's biological activity.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2018.06.059