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DC Field | Value | Language |
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dc.citation.endPage | 3748 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 3743 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 110 | - |
dc.contributor.author | Hyung, Suk-Joon | - |
dc.contributor.author | DeToma, Alaina S. | - |
dc.contributor.author | Brender, Jeffrey R. | - |
dc.contributor.author | Lee, Sanghyun | - |
dc.contributor.author | Vivekanandan, Subramanian | - |
dc.contributor.author | Kochi, Akiko | - |
dc.contributor.author | Choi, Jung-Suk | - |
dc.contributor.author | Ramamoorthy, Ayyalusamy | - |
dc.contributor.author | Ruotolo, Brandon T. | - |
dc.contributor.author | Lim, Mi Hee | - |
dc.date.accessioned | 2023-12-22T04:10:02Z | - |
dc.date.available | 2023-12-22T04:10:02Z | - |
dc.date.created | 2014-11-11 | - |
dc.date.issued | 2013-03 | - |
dc.description.abstract | Despite the significance of Alzheimer's disease, the link between metal-associated amyloid-β (metal-Aβ) and disease etiology remains unclear. To elucidate this relationship, chemical tools capable of specifically targeting and modulating metal-Aβ species are necessary, along with a fundamental understanding of their mechanism at the molecular level. Herein, we investigated and compared the interactions and reactivities of the green tea extract, (-)-epigallocatechin-3-gallate [(2R,3R)-5,7-dihydroxy-2- (3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3-yl 3,4,5- trihydroxybenzoate; EGCG], with metal [Cu(II) and Zn(II)]-Aβ and metal-free Aβ species. We found that EGCG interacted with metal-Aβ species and formed small, unstructured Aβ aggregates more noticeably than in metal-free conditions in vitro. In addition, upon incubation with EGCG, the toxicity presented by metalfree Aβ and metal-Aβ was mitigated in living cells. To understand this reactivity at the molecular level, structural insights were obtained by ion mobility-mass spectrometry (IM-MS), 2D NMR spectroscopy, and computational methods. These studies indicated that (i) EGCG was bound to Aβ monomers and dimers, generating more compact peptide conformations than those from EGCGuntreated Aβ species; and (ii) ternary EGCG-metal-Aβ complexes were produced. Thus, we demonstrate the distinct antiamyloidogenic reactivity of EGCG toward metal-Aβ species with a structurebased mechanism. | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.110, no.10, pp.3743 - 3748 | - |
dc.identifier.doi | 10.1073/pnas.1220326110 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.scopusid | 2-s2.0-84874609836 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/8612 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84874609836 | - |
dc.identifier.wosid | 000316377400027 | - |
dc.language | 영어 | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.title | Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-beta species |
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dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | amyloid-beta peptide | - |
dc.subject.keywordAuthor | metal ions | - |
dc.subject.keywordAuthor | natural products | - |
dc.subject.keywordAuthor | amyloidogenesis | - |
dc.subject.keywordPlus | MEROZOITE SURFACE PROTEIN-2 | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | MASS-SPECTROMETRY | - |
dc.subject.keywordPlus | EPIGALLOCATECHIN GALLATE | - |
dc.subject.keywordPlus | FIBRIL FORMATION | - |
dc.subject.keywordPlus | ZINC-BINDING | - |
dc.subject.keywordPlus | AGGREGATION | - |
dc.subject.keywordPlus | EGCG | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | POLYPEPTIDE | - |
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