Vault nanoparticles engineered with the protein transduction domain, TAT48, enhances cellular uptake.
Vaults are naturally-occurring ribonucleoprotein particles found in nearly all eukaryotic cells. They were named for their morphological resemblance to the vaulted ceilings of gothic cathedrals. These ubiquitous nanoparticles are quite abundant with 10(4)-10(6) copies found in the cytoplasm depending on cell type. The structural shell of the particle can self-assemble from 78 copies of a single protein, the major vault protein. This finding has allowed vaults to be bioengineered, resulting in a variety of new functions and capabilities directed toward overcoming many limitations posed by current gene and drug delivery systems. In this study, we demonstrate that recombinant vaults, with the addition of a cell penetration peptide, TAT, can be rapidly delivered to cells in vitro with significantly elevated binding and uptake efficiency. This TAT-vault nanoparticle could be a valuable tool for improving the retention and penetration of therapeutic drugs at tumor sites.
Department of Biological Chemistry, David Geffen School of Medicine at UCLA, Los Angeles, California 90095, USA.
Jian
J
Yang
Aswin
A
Srinivasan
Yang
Y
Sun
Jan
J
Mrazek
Zhanyong
Z
Shu
Valerie A
VA
Kickhoefer
Leonard H
LH
Rome
D045744:Cell Line, Tumor; D006367:HeLa Cells; D006801:Humans; D053758:Nanoparticles / Q000737:chemistry* / Q000648:ultrastructure; D009374:Neoplasms, Experimental / Q000378:metabolism* / Q000473:pathology; D010316:Particle Size; D015202:Protein Engineering / Q000379:methods*; D020394:Vault Ribonucleoprotein Particles / Q000737:chemistry / Q000235:genetics* / Q000493:pharmacokinetics*
D020394:Vault Ribonucleoprotein Particles