Solid-state nanopore analysis on conformation change of p53TAD-MDM2 fusion protein induced by protein-protein interaction

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dc.contributor.authorH Chae-
dc.contributor.authorDong-Kyu Kwak-
dc.contributor.authorMi-Kyung Lee-
dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorK B Kim-
dc.date.accessioned2018-10-24T16:30:35Z-
dc.date.available2018-10-24T16:30:35Z-
dc.date.issued2018-
dc.identifier.issn20403364-
dc.identifier.uri10.1039/c8nr06423gko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/18087-
dc.description.abstractAlthough protein-protein interactions (PPIs) are emerging therapeutic targets for human diseases, development of high-throughput screening (HTS) technologies against PPI targets remains challenging. In this study, we propose a protein complex structure to effectively detect conformational changes of protein resulting from PPI using solid-state nanopore for a novel, widely-applicable drug screening method against various PPI targets. To effectively detect conformational changes resulting from PPI, we designed a fusion protein MLP (MDM2-linker-p53TAD), where p53TAD and MDM2 are connected by a 16 amino acid linker. The globular conformation of MLP exhibited a single-peak translocation event, whereas the dumbbell-like conformation of nutlin-3-bound MLP revealed as a double-peak signal. The proportion of double-peak to single-peak signals increased from 9.3% to 23.0% as nutlin-3 concentration increased. The translocation kinetics of the two different MLP conformations with varied applied voltage were analyzed. Further, the fractional current of the intra-peak of the double-peak signal was analyzed, probing the structure of our designed protein complex. This approach of nanopore sensing may be extendedly employed in screening of PPI inhibitors and protein conformation studies.-
dc.publisherRoyal Soc Chem-
dc.titleSolid-state nanopore analysis on conformation change of p53TAD-MDM2 fusion protein induced by protein-protein interaction-
dc.title.alternativeSolid-state nanopore analysis on conformation change of p53TAD-MDM2 fusion protein induced by protein-protein interaction-
dc.typeArticle-
dc.citation.titleNanoscale-
dc.citation.number36-
dc.citation.endPage17235-
dc.citation.startPage17227-
dc.citation.volume10-
dc.contributor.affiliatedAuthorMi-Kyung Lee-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.alternativeName최홍식-
dc.contributor.alternativeName곽동규-
dc.contributor.alternativeName이미경-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName김기범-
dc.identifier.bibliographicCitationNanoscale, vol. 10, no. 36, pp. 17227-17235-
dc.identifier.doi10.1039/c8nr06423g-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
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