Noncovalent protein transduction in plant cells by macropinocytosis.
* Protein delivery across cellular membranes or compartments is primarily limited by low biomembrane permeability. * Many protein transduction domains (PTDs) have previously been generated, and covalently cross-linked with cargoes for cellular internalization. * An arginine-rich intracellular delivery (AID) peptide could rapidly deliver fluorescent proteins or beta-galactosidase enzyme into plant and animal cells in a noncovalent fashion. The possible mechanism of this noncovalent protein transduction (NPT) may involve macropinocytosis. * The NPT via a nontoxic AID peptide provides a powerful tool characterized by its simplicity and quickness to have active proteins function in living cells in vivo. This should be of broad utility for functional enzyme assays and protein therapies in both plant biology research as well as biomedical applications.
Chang
Microsugar
M
Department of Life Science, National Dong Hwa University, Hualien 97401, Taiwan.
Chou
Jyh-Ching
JC
Department of Life Science, National Dong Hwa University, Hualien 97401, Taiwan.
Chen
Chung-Pin
CP
Department of Life Science, National Dong Hwa University, Hualien 97401, Taiwan.
Liu
Betty Revon
BR
Department of Life Science, National Dong Hwa University, Hualien 97401, Taiwan.
Lee
Han-Jung
HJ
Department of Life Science, National Dong Hwa University, Hualien 97401, Taiwan.
D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D045744:Cell Line, Tumor; D003584:Cytological Techniques / Q000379:methods; D006801:Humans; D019697:Onions / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D010873:Pinocytosis; D010944:Plants / Q000378:metabolism*; D010957:Plasmids; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D011506:Proteins / Q000378:metabolism; D003313:Zea mays / Q000378:metabolism
D002352:Carrier Proteins; D010455:Peptides; D011506:Proteins