DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ryu, Jungki | ko |
dc.contributor.author | Girigoswami, Koyeli | ko |
dc.contributor.author | Ha, Chanki | ko |
dc.contributor.author | Ku, Sook Hee | ko |
dc.contributor.author | Park, Chan Beum | ko |
dc.date.accessioned | 2008-07-15T01:31:25Z | - |
dc.date.available | 2008-07-15T01:31:25Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2008-05 | - |
dc.identifier.citation | BIOCHEMISTRY, v.47, no.19, pp.5328 - 5335 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | http://hdl.handle.net/10203/5801 | - |
dc.description.abstract | Recently discovered evidences suggest that precipitation of Alzheimer's beta-amyloid (A beta) peptide and the toxicity in Alzheimer's disease (AD) are caused by abnormal interactions with neocortical metal ions, especially Zn2+, CU2+, and Fe3+. While many studies had focused on the role of a "single" metal ion and its interaction with A beta peptides, such studies involving "multiple" metal ions have hardly been explored. Here, to explore the nature of codeposition of different metals, two or more metal ions along with A beta were incubated over a solid template prepared by immobilizing A beta 42 oligomers. The influence of Zn2+, Cu2+, and Fe3+ on A beta aggregation was investigated by two approaches: co-incubation and sequential addition. Our results using ex situ AFM, ThT-induced fluorescence, and FTIR spectroscopy indicated that the co-incubation of Cu2+, Zn2+, and Fe3+ significantly altered the morphology of aggregates. A concentration dependence study with mixed metal ions suggested that Zn2+ was required at much lower concentrations than CU2+ to yield nonfibrillar amorphous A beta deposits. In addition, sequential addition of Zn2+ or Cu2+ on fibrillar aggregates formed by Fe3+ demonstrated that Zn2+ and Cu2+ could possibly change the conformation of the aggregates induced by Fe3+. Our findings elucidate the coexistence of multiple metal ions through their interactions with A beta peptides or its aggregates. | - |
dc.description.sponsorship | This study was supported by grants from the Korea Research Foundation (KRF-2006-D00078) and the National Institute of Health (1R21AG024114-01A2). | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | Amer Chemical Soc | - |
dc.subject | SENILE PLAQUE CORES | - |
dc.subject | ALZHEIMER A-BETA | - |
dc.subject | IN-VITRO | - |
dc.subject | COPPER-BINDING | - |
dc.subject | DISEASE | - |
dc.subject | ZINC | - |
dc.subject | PEPTIDE | - |
dc.subject | FIBRIL | - |
dc.subject | IRON | - |
dc.subject | A-BETA(1-42) | - |
dc.title | Influence of multiple metal ions on beta-amyloid aggregation and dissociation on a solid surface | - |
dc.type | Article | - |
dc.identifier.wosid | 000255547600009 | - |
dc.identifier.scopusid | 2-s2.0-43249119241 | - |
dc.type.rims | ART | - |
dc.citation.volume | 47 | - |
dc.citation.issue | 19 | - |
dc.citation.beginningpage | 5328 | - |
dc.citation.endingpage | 5335 | - |
dc.citation.publicationname | BIOCHEMISTRY | - |
dc.identifier.doi | 10.1021/bi800012e | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Park, Chan Beum | - |
dc.contributor.nonIdAuthor | Ryu, Jungki | - |
dc.contributor.nonIdAuthor | Girigoswami, Koyeli | - |
dc.contributor.nonIdAuthor | Ha, Chanki | - |
dc.contributor.nonIdAuthor | Ku, Sook Hee | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | SENILE PLAQUE CORES | - |
dc.subject.keywordPlus | ALZHEIMER A-BETA | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | COPPER-BINDING | - |
dc.subject.keywordPlus | DISEASE | - |
dc.subject.keywordPlus | ZINC | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | FIBRIL | - |
dc.subject.keywordPlus | IRON | - |
dc.subject.keywordPlus | A-BETA(1-42) | - |
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