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A protein transduction domain located at the NH2-terminus of human translationally controlled tumor protein for delivery of active molecules to cells

Title
A protein transduction domain located at the NH2-terminus of human translationally controlled tumor protein for delivery of active molecules to cells
Authors
Kim M.Kim H.Y.Kim S.Jung J.Maeng J.Chang J.Lee K.
Ewha Authors
이경림장준맹지혜
SCOPUS Author ID
이경림scopus; 장준scopus; 맹지혜scopus
Issue Date
2011
Journal Title
Biomaterials
ISSN
0142-9612JCR Link
Citation
vol. 32, no. 1, pp. 222 - 230
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Protein transduction domains (PTDs) are small peptides, able to penetrate biological membranes and deliver various types of cargo both in vitro and in vivo. Because use of PTDs originating from viral origins resulted in undesired effects, PTDs originating from non-viral origins are needed. Here, we report that a 10-amino acid peptide (MIIYRDLISH) derived from the NH2-terminus of human translationally controlled tumor protein (TCTP) functions as a PTD. This peptide was internalized through lipid raft-dependent endocytosis and partial macropinocytosis, and did not enter lysosome and nucleus. Beta-galactosidase fused to TCTP-PTD, when injected into mice, was efficiently delivered to liver, kidney, spleen, heart, and lungs of the animals. Preincubation of TCTP-PTD with adenovirus increased adenoviral mediated-gene expression in cells and also improved immune response to intranasally administered adenovirus expressing the triple repeat of G glycoprotein of respiratory syncytial virus (RSV), rAd/3×G. These findings suggest that TCTP-PTD might overcome the limitations of polycation-mediated transduction and serve as an efficient vehicle for drug delivery. © 2010 Elsevier Ltd.
DOI
10.1016/j.biomaterials.2010.08.077
Appears in Collections:
약학대학 > 약학과 > Journal papers
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