DC Field | Value | Language |
---|---|---|
dc.contributor.author | Choi, Tae Su | ko |
dc.contributor.author | Lee, Hyuck Jin | ko |
dc.contributor.author | Han, Jong Yoon | ko |
dc.contributor.author | Lim, Mi Hee | ko |
dc.contributor.author | Kim, Hugh I. | ko |
dc.date.accessioned | 2018-02-21T06:05:36Z | - |
dc.date.available | 2018-02-21T06:05:36Z | - |
dc.date.created | 2018-02-08 | - |
dc.date.created | 2018-02-08 | - |
dc.date.issued | 2017-11 | - |
dc.identifier.citation | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.139, no.43, pp.15437 - 15445 | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.uri | http://hdl.handle.net/10203/240253 | - |
dc.description.abstract | Regulation of amyloid-beta (A beta) 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-A beta interactions and A beta 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), A beta, and HSA, which is able to alter the aggregation and cytotoxicity of A beta peptides and induce their cellular transportation. In addition, a single A beta monomer-bound HSA is observed with the structural change of A beta from a random coil to an alpha-helix. Small-angle X-ray scattering (SAXS) studies indicate that A beta-HSA complexation causes no structural variation of HSA in solution. Conversely, ion mobility mass spectrometry (IM-MS) results present that A beta 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 A beta 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 A beta while maintaining A beta-HSA interaction. Therefore, HSA is capable of controlling metal-free and metal-bound A beta aggregation and aiding the cellular transportation of A beta via A beta-HSA complexation. The overall results and observations regarding HSA, A beta, and metal ions advance our knowledge of how protein-protein interactions associated with A beta and metal ions could be linked to AD pathogenesis. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | A-BETA-PEPTIDE | - |
dc.subject | MODERATE ALZHEIMERS-DISEASE | - |
dc.subject | MOBILITY-MASS SPECTROMETRY | - |
dc.subject | PARTIALLY FOLDED STRUCTURE | - |
dc.subject | METAL-IONS | - |
dc.subject | MECHANISTIC INSIGHTS | - |
dc.subject | PROTEIN AGGREGATION | - |
dc.subject | PLASMA-EXCHANGE | - |
dc.subject | SENILE PLAQUES | - |
dc.subject | IN-VITRO | - |
dc.title | Molecular Insights into Human Serum Albumin as a Receptor of Amyloid-beta in the Extracellular Region | - |
dc.type | Article | - |
dc.identifier.wosid | 000414506400027 | - |
dc.identifier.scopusid | 2-s2.0-85032628332 | - |
dc.type.rims | ART | - |
dc.citation.volume | 139 | - |
dc.citation.issue | 43 | - |
dc.citation.beginningpage | 15437 | - |
dc.citation.endingpage | 15445 | - |
dc.citation.publicationname | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | - |
dc.identifier.doi | 10.1021/jacs.7b08584 | - |
dc.contributor.localauthor | Lim, Mi Hee | - |
dc.contributor.nonIdAuthor | Choi, Tae Su | - |
dc.contributor.nonIdAuthor | Lee, Hyuck Jin | - |
dc.contributor.nonIdAuthor | Han, Jong Yoon | - |
dc.contributor.nonIdAuthor | Kim, Hugh I. | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | A-BETA-PEPTIDE | - |
dc.subject.keywordPlus | MODERATE ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | MOBILITY-MASS SPECTROMETRY | - |
dc.subject.keywordPlus | PARTIALLY FOLDED STRUCTURE | - |
dc.subject.keywordPlus | METAL-IONS | - |
dc.subject.keywordPlus | MECHANISTIC INSIGHTS | - |
dc.subject.keywordPlus | PROTEIN AGGREGATION | - |
dc.subject.keywordPlus | PLASMA-EXCHANGE | - |
dc.subject.keywordPlus | SENILE PLAQUES | - |
dc.subject.keywordPlus | IN-VITRO | - |
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