Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88105
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dc.contributor.authorYu, Kangen
dc.contributor.authorYau, Yin Hoeen
dc.contributor.authorSinha, Ameyaen
dc.contributor.authorTan, Tabithaen
dc.contributor.authorKickhoefer, Valerie A.en
dc.contributor.authorRome, Leonard H.en
dc.contributor.authorLee, Hwankyuen
dc.contributor.authorShochat, Susana G.en
dc.contributor.authorLim, Sierinen
dc.date.accessioned2018-08-20T06:40:28Zen
dc.date.accessioned2019-12-06T16:56:06Z-
dc.date.available2018-08-20T06:40:28Zen
dc.date.available2019-12-06T16:56:06Z-
dc.date.issued2017en
dc.identifier.citationYu, 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-xen
dc.identifier.issn2045-2322en
dc.identifier.urihttps://hdl.handle.net/10356/88105-
dc.description.abstractVaults 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.en
dc.format.extent10 p.en
dc.language.isoenen
dc.relation.ispartofseriesScientific Reportsen
dc.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/.en
dc.subjectMolecular Releaseen
dc.subjectVaulten
dc.subjectDRNTU::Engineering::Bioengineeringen
dc.titleModulation of the vault protein-protein interaction for tuning of molecular releaseen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen
dc.contributor.schoolSchool of Materials Science & Engineeringen
dc.contributor.schoolSchool of Biological Sciencesen
dc.contributor.researchNTU-Northwestern Institute for Nanomedicineen
dc.identifier.doi10.1038/s41598-017-12870-xen
dc.description.versionPublished versionen
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