Premium
Noncovalent protein transduction in plant cells by macropinocytosis
Author(s) -
Chang Microsugar,
Chou JyhChing,
Chen ChungPin,
Liu Betty Revon,
Lee HanJung
Publication year - 2007
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.2007.01977.x
Subject(s) - pinocytosis , transduction (biophysics) , internalization , microbiology and biotechnology , signal transduction , biology , biochemistry , protein–protein interaction , intracellular , peptide , chemistry , endocytosis , cell
Summary• 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.