Immobilization of recombinant vault nanoparticles on solid substrates

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...

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Main 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.
Other Authors: School of Materials Science & Engineering
Format: Article
Language:English
Published: 2012
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Online Access:https://hdl.handle.net/10356/93974
http://hdl.handle.net/10220/8608
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-939742020-06-01T10:13:44Z Immobilization of recombinant vault nanoparticles on solid substrates 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. School of Materials Science & Engineering DRNTU::Engineering::Materials 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. 2012-09-24T01:34:30Z 2019-12-06T18:48:39Z 2012-09-24T01:34:30Z 2019-12-06T18:48:39Z 2010 2010 Journal Article 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. 1936-0851 https://hdl.handle.net/10356/93974 http://hdl.handle.net/10220/8608 10.1021/nn901167s en ACS nano © 2010 American Chemical Society.
institution Nanyang Technological University
building NTU Library
country Singapore
collection DR-NTU
language English
topic DRNTU::Engineering::Materials
spellingShingle DRNTU::Engineering::Materials
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.
Immobilization of recombinant vault nanoparticles on solid substrates
description 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.
author2 School of Materials Science & Engineering
author_facet School of Materials Science & Engineering
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.
format Article
author 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.
author_sort Xia, Yun
title Immobilization of recombinant vault nanoparticles on solid substrates
title_short Immobilization of recombinant vault nanoparticles on solid substrates
title_full Immobilization of recombinant vault nanoparticles on solid substrates
title_fullStr Immobilization of recombinant vault nanoparticles on solid substrates
title_full_unstemmed Immobilization of recombinant vault nanoparticles on solid substrates
title_sort immobilization of recombinant vault nanoparticles on solid substrates
publishDate 2012
url https://hdl.handle.net/10356/93974
http://hdl.handle.net/10220/8608
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