| Literature DB >> 17335496 |
Microsugar Chang1, Jyh-Ching Chou1, Chung-Pin Chen1, Betty Revon Liu1, Han-Jung Lee1.
Abstract
* 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.Entities:
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Year: 2007 PMID: 17335496 DOI: 10.1111/j.1469-8137.2007.01977.x
Source DB: PubMed Journal: New Phytol ISSN: 0028-646X Impact factor: 10.151