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 β-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. © The Authors (2007). Journal Compilation © New Phytologist (2007).
CITATION STYLE
Chang, M., Chou, J. C., Chen, C. P., Liu, B. R., & Lee, H. J. (2007). Noncovalent protein transduction in plant cells by macropinocytosis. New Phytologist, 174(1), 46–56. https://doi.org/10.1111/j.1469-8137.2007.01977.x
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