Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/93974
Title: Immobilization of recombinant vault nanoparticles on solid substrates
Authors: Xia, Yun
Ramgopal, Yamini
Li, Hai
Shang, Lei
Srinivas, Parisa
Kickhoefer, Valerie A.
Rome, Leonard H.
Preiser, Peter Rainer
Boey, Freddy Yin Chiang
Zhang, Hua
Venkatraman, Subbu S.
Keywords: DRNTU::Engineering::Materials
Issue Date: 2010
Source: Xia, Y., Ramgopal, Y., Li, H., Shang, L., Srinivas, P., Kickhoefer, V. A., et al. (2010). Immobilization of recombinant vault nanoparticles on solid substrates. ACS Nano, 4(3), 1417-1424.
Series/Report no.: ACS nano
Abstract: Native vaults are nanoscale particles found abundantly in the cytoplasm of most eukaryotic cells. They have a capsule-like structure with a thin shell surrounding a “hollow” interior compartment. Recombinant vault particles were found to self-assemble following expression of the major vault protein (MVP) in a baculovirus expression system, and these particles are virtually identical to native vaults. Such particles have been recently studied as potential delivery vehicles. In this study, we focus on immobilization of vault particles on a solid substrate, such as glass, as a first step to study their interactions with cells. To this end, we first engineered the recombinant vaults by fusing two different tags to the C-terminus of MVP, a 3 amino acid RGD peptide and a 12 amino acid RGD-strep-tag peptide. We have demonstrated two strategies for immobilizing vaults on solid substrates. The barrel-and-cap structure of vault particles was observed for the first time, by atomic force microscopy (AFM), in a dry condition. This work proved the feasibility of immobilizing vault nanoparticles on a material surface, and the possibility of using vault nanoparticles as localized and sustainable drug carriers as well as a biocompatible surface moiety.
URI: https://hdl.handle.net/10356/93974
http://hdl.handle.net/10220/8608
ISSN: 1936-0851
DOI: 10.1021/nn901167s
Rights: © 2010 American Chemical Society.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:MSE Journal Articles

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