Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88105
Title: Modulation of the vault protein-protein interaction for tuning of molecular release
Authors: Yu, Kang
Yau, Yin Hoe
Sinha, Ameya
Tan, Tabitha
Kickhoefer, Valerie A.
Rome, Leonard H.
Lee, Hwankyu
Shochat, Susana G.
Lim, Sierin
Keywords: Molecular Release
Vault
DRNTU::Engineering::Bioengineering
Issue Date: 2017
Source: Yu, K., Yau, Y. H., Sinha, A., Tan, T., Kickhoefer, V. A., Rome, L. H., . . . Lim, S. (2017). Modulation of the vault protein-protein interaction for tuning of molecular release. Scientific Reports, 7, 14816-. doi:10.1038/s41598-017-12870-x
Series/Report no.: Scientific Reports
Abstract: Vaults are naturally occurring ovoid nanoparticles constructed from a protein shell that is composed of multiple copies of major vault protein (MVP). The vault-interacting domain of vault poly(ADP-ribose)-polymerase (INT) has been used as a shuttle to pack biomolecular cargo in the vault lumen. However, the interaction between INT and MVP is poorly understood. It is hypothesized that the release rate of biomolecular cargo from the vault lumen is related to the interaction between MVP and INT. To tune the release of molecular cargos from the vault nanoparticles, we determined the interactions between the isolated INT-interacting MVP domains (iMVP) and wild-type INT and compared them to two structurally modified INT: 15-amino acid deletion at the C terminus (INTΔC15) and histidine substituted at the interaction surface (INT/DSA/3 H) to impart a pH-sensitive response. The apparent affinity constants determined using surface plasmon resonance (SPR) biosensor technology are 262 ± 4 nM for iMVP/INT, 1800 ± 160 nM for iMVP/INTΔC15 at pH 7.4. The INT/DSA/3 H exhibits stronger affinity to iMVP (K Dapp = 24 nM) and dissociates at a slower rate than wild-type INT at pH 6.0.
URI: https://hdl.handle.net/10356/88105
http://hdl.handle.net/10220/45629
ISSN: 2045-2322
DOI: http://dx.doi.org/10.1038/s41598-017-12870-x
Rights: © 2017 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. Te images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SCBE Journal Articles

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