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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.

Vault particles possess many attributes that can be exploited in nanobiotechnology, particularly in the creation of drug delivery nanodevices. These include self-assembly, 100 nm size range, a dynamic structure that may be controlled for manipulation of drug release kinetics and natural presence in humans ensuring biocompatibility. The flexibility and the adaptability of this system have been greatly enhanced by the emerging atomic-level information and improved comprehension of vault structure and dynamics. It seems likely that this information will allow their specific tailoring to the individual requirements of each drug and target tissue. These properties provide vaults with an enormous potential as a versatile delivery platform., (Copyright © 2012 Elsevier Ltd. All rights reserved.)