Competitive homo- and hetero- self-assembly of amyloid-beta 1-42 and 1-40 in the early stage of fibrillation
DC Field | Value | Language |
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dc.contributor.author | Heo, Chae Eun | - |
dc.contributor.author | Choi, Tae Su | - |
dc.contributor.author | Kim, Hugh I. | - |
dc.date.accessioned | 2021-09-02T11:45:32Z | - |
dc.date.available | 2021-09-02T11:45:32Z | - |
dc.date.created | 2021-06-19 | - |
dc.date.issued | 2018-05 | - |
dc.identifier.issn | 1387-3806 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/75620 | - |
dc.description.abstract | Amyloid-beta 1-42 (A beta 42) and 1-40 (A beta 40) peptides, whose self-assembly process has been linked with the formation of amyloid plaques in Alzheimer's disease, exist as a mixture in human fluids. For this reason, heteromeric self-assembly of A beta 42 and A beta 40 has been widely investigated to understand the influence of this mixture in A$ fibrillation. However, understanding the role of heteromeric self-assembly in A beta fibrillation is a challenge owing to the heterogeneous cross-interactions between A beta 42 and A beta 40. Herein, we demonstrated the influence of the cross-interaction of A beta 42 and A beta 40 in the early stage of fibrillation using electrospray ionization mass spectrometry (ESI-MS) and drift tube ion mobility spectrometry (DTIMS) along with solution small-angle X-ray scattering (SAXS) and molecular dynamics (MD) simulations. In the mixture of A beta 42 and A beta 40, A beta 42 has only a slight preference for homo-oligomerization versus hetero-oligomerization with A beta 40 (similar to 1-2 fold) when forming small oligomers (from dimer to tetramer) in the early stage of fibrillation. However, the cross-interaction is gradually attenuated as oligomerization proceeds because of the different conformations in the A beta 42 and A beta 40 assemblies. Consequently, the competitive self-assembly of A beta 42 and A beta 40 can disturb the homo-oligomerization of A beta 42 in the early stage of fibrillation, whereas A beta 42 and A beta 40 species prefer the independent self-assembly after the early stage. (C) 2018 Elsevier B.V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | MOBILITY-MASS-SPECTROMETRY | - |
dc.subject | ATOMIC-RESOLUTION STRUCTURE | - |
dc.subject | ALZHEIMERS-DISEASE | - |
dc.subject | GAS-PHASE | - |
dc.subject | FIBRILS | - |
dc.subject | OLIGOMERS | - |
dc.subject | A-BETA-42 | - |
dc.subject | PEPTIDE | - |
dc.subject | A-BETA(1-42) | - |
dc.subject | COMPLEXES | - |
dc.title | Competitive homo- and hetero- self-assembly of amyloid-beta 1-42 and 1-40 in the early stage of fibrillation | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Hugh I. | - |
dc.identifier.doi | 10.1016/j.ijms.2018.02.002 | - |
dc.identifier.scopusid | 2-s2.0-85042327962 | - |
dc.identifier.wosid | 000429948400003 | - |
dc.identifier.bibliographicCitation | INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, v.428, pp.15 - 21 | - |
dc.relation.isPartOf | INTERNATIONAL JOURNAL OF MASS SPECTROMETRY | - |
dc.citation.title | INTERNATIONAL JOURNAL OF MASS SPECTROMETRY | - |
dc.citation.volume | 428 | - |
dc.citation.startPage | 15 | - |
dc.citation.endPage | 21 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Physics | - |
dc.relation.journalResearchArea | Spectroscopy | - |
dc.relation.journalWebOfScienceCategory | Physics, Atomic, Molecular & Chemical | - |
dc.relation.journalWebOfScienceCategory | Spectroscopy | - |
dc.subject.keywordPlus | MOBILITY-MASS-SPECTROMETRY | - |
dc.subject.keywordPlus | ATOMIC-RESOLUTION STRUCTURE | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | GAS-PHASE | - |
dc.subject.keywordPlus | FIBRILS | - |
dc.subject.keywordPlus | OLIGOMERS | - |
dc.subject.keywordPlus | A-BETA-42 | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | A-BETA(1-42) | - |
dc.subject.keywordPlus | COMPLEXES | - |
dc.subject.keywordAuthor | Alzheimer&apos | - |
dc.subject.keywordAuthor | s disease | - |
dc.subject.keywordAuthor | Cross-interaction | - |
dc.subject.keywordAuthor | Electrospray ionization-mass spectrometry | - |
dc.subject.keywordAuthor | Solution small-angle X-ray scattering | - |
dc.subject.keywordAuthor | Drift tube ion mobility spectrometry | - |
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