Metal ions affect the formation and stability of amyloid aggregates at multiple length scales
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Myeongsang | - |
dc.contributor.author | Kim, Jae In | - |
dc.contributor.author | Na, Sungsoo | - |
dc.contributor.author | Eom, Kilho | - |
dc.date.accessioned | 2021-09-02T12:43:32Z | - |
dc.date.available | 2021-09-02T12:43:32Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2018-04-07 | - |
dc.identifier.issn | 1463-9076 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/76154 | - |
dc.description.abstract | Amyloid beta (A beta) aggregates, which are a hallmark for neurodegenerative disease, are formed through a self-assembly process such as aggregation of A beta peptide chains. This aggregation process depends on the solvent conditions under which the proteins are aggregated. Nevertheless, the underlying mechanism of the ionic effect on the formation and stability of amyloid aggregates has not been fully understood. Here, we report how metal ions play a role in the formation and stability of A beta aggregates at different length scales, i.e. oligomers and fibrils. It is shown that the metal (i.e. zinc or copper) ion increases the stability of A beta oligomers, whereas the metal ion reduces the stability of A fibrils. In addition, we found that zinc ions are able to more effectively destabilize fibril structures than copper ions. Metal ion-mediated (de)stabilization of A beta oligomers (or fibrils) is attributed to the critical effect of the metal ion on the beta-sheet rich crystalline structure of the amyloid aggregate and the status of hydrogen bonds within the aggregate. Our study sheds light on the role of the metal ion in stabilizing the amyloid oligomers known as a toxic agent (to functional cells), which is consistent with clinical observation that high concentrations of metal ions are found in patients suffering from neurodegenerative diseases. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ROYAL SOC CHEMISTRY | - |
dc.subject | MOLECULAR-DYNAMICS | - |
dc.subject | A-BETA | - |
dc.subject | CONFORMATIONAL-CHANGES | - |
dc.subject | MECHANICAL-PROPERTIES | - |
dc.subject | ALZHEIMERS | - |
dc.subject | FIBRILS | - |
dc.subject | PEPTIDE | - |
dc.subject | BINDING | - |
dc.subject | ZINC | - |
dc.subject | RAT | - |
dc.title | Metal ions affect the formation and stability of amyloid aggregates at multiple length scales | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Na, Sungsoo | - |
dc.identifier.doi | 10.1039/c7cp05072k | - |
dc.identifier.scopusid | 2-s2.0-85044840604 | - |
dc.identifier.wosid | 000428779700058 | - |
dc.identifier.bibliographicCitation | PHYSICAL CHEMISTRY CHEMICAL PHYSICS, v.20, no.13, pp.8951 - 8961 | - |
dc.relation.isPartOf | PHYSICAL CHEMISTRY CHEMICAL PHYSICS | - |
dc.citation.title | PHYSICAL CHEMISTRY CHEMICAL PHYSICS | - |
dc.citation.volume | 20 | - |
dc.citation.number | 13 | - |
dc.citation.startPage | 8951 | - |
dc.citation.endPage | 8961 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Physics | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Physical | - |
dc.relation.journalWebOfScienceCategory | Physics, Atomic, Molecular & Chemical | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | A-BETA | - |
dc.subject.keywordPlus | CONFORMATIONAL-CHANGES | - |
dc.subject.keywordPlus | MECHANICAL-PROPERTIES | - |
dc.subject.keywordPlus | ALZHEIMERS | - |
dc.subject.keywordPlus | FIBRILS | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | ZINC | - |
dc.subject.keywordPlus | RAT | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.