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DC Field | Value | Language |
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dc.citation.endPage | 15445 | - |
dc.citation.number | 43 | - |
dc.citation.startPage | 15437 | - |
dc.citation.title | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | - |
dc.citation.volume | 139 | - |
dc.contributor.author | Choi, Tae Su | - |
dc.contributor.author | Lee, Hyuck Jin | - |
dc.contributor.author | Han, Jong Yoon | - |
dc.contributor.author | Lim, Mi Hee | - |
dc.contributor.author | Kim, Hugh I. | - |
dc.date.accessioned | 2023-12-21T21:38:09Z | - |
dc.date.available | 2023-12-21T21:38:09Z | - |
dc.date.created | 2017-11-21 | - |
dc.date.issued | 2017-11 | - |
dc.description.abstract | Regulation of amyloid-β (Aβ) aggregation by metal ions and proteins is essential for understanding the pathology of Alzheimer’s disease (AD). Human serum albumin (HSA), a regulator of metal and protein transportation, can modulate metal-Aβ interactions and Aβ aggregation in human fluid; however, the molecular mechanisms for such activities remain unclear. Herein, we report the molecular-level complexation between Zn(II), Cu(II), Aβ, and HSA, which is able to alter the aggregation and cytotoxicity of Aβ peptides and induce their cellular transportation. In addition, a single Aβ monomer-bound HSA is observed with the structural change of Aβ from a random coil to an α-helix. Small-angle X-ray scattering (SAXS) studies indicate that Aβ-HSA complexation causes no structural variation of HSA in solution. Conversely, ion mobility mass spectrometry (IM-MS) results present that Aβ prevents the shrinkage of the V-shaped groove of HSA in the gas phase. Consequently, for the first time, HSA is demonstrated to predominantly capture a single Aβ monomer at the groove using the phase transfer of a protein heterodimer from solution to the gas phase. Moreover, HSA sequesters Zn(II) and Cu(II) from Aβ while maintaining Aβ-HSA interaction. Therefore, HSA is capable of controlling metal-free and metal-bound Aβ aggregation and aiding the cellular transportation of Aβ via Aβ-HSA complexation. The overall results and observations regarding HSA, Aβ, and metal ions advance our knowledge of how protein-protein interactions associated with Aβ and metal ions could be linked to AD pathogenesis. | - |
dc.identifier.bibliographicCitation | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.139, no.43, pp.15437 - 15445 | - |
dc.identifier.doi | 10.1021/jacs.7b08584 | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.scopusid | 2-s2.0-85032628332 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/22954 | - |
dc.identifier.url | http://pubs.acs.org/doi/abs/10.1021/jacs.7b08584 | - |
dc.identifier.wosid | 000414506400027 | - |
dc.language | 영어 | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Molecular Insights into Human Serum Albumin as a Receptor of Amyloid-β in the Extracellular Region | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | MOBILITY-MASS SPECTROMETRY | - |
dc.subject.keywordPlus | PARTIALLY FOLDED STRUCTURE | - |
dc.subject.keywordPlus | A-BETA | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | METAL-IONS | - |
dc.subject.keywordPlus | MECHANISTIC INSIGHTS | - |
dc.subject.keywordPlus | PLASMA-EXCHANGE | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | PROTEIN | - |
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