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DC Field | Value | Language |
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dc.citation.endPage | 1653 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 1645 | - |
dc.citation.title | CHEMISTRY-A EUROPEAN JOURNAL | - |
dc.citation.volume | 23 | - |
dc.contributor.author | Kang, Juhye | - |
dc.contributor.author | Lee, Shin Jung C. | - |
dc.contributor.author | Nam. Jung Seung | - |
dc.contributor.author | Lee, Hyuck Jin | - |
dc.contributor.author | Kang, Mueong-G. | - |
dc.contributor.author | Korshavn, Kyle J. | - |
dc.contributor.author | Kim, Hyun-Tak | - |
dc.contributor.author | Cho, Jaeheung | - |
dc.contributor.author | Ramamoorthy, Ayyalusamy | - |
dc.contributor.author | Rhee, Hyun-Woo | - |
dc.contributor.author | Kwon, Tae-Hyuk | - |
dc.contributor.author | Lim, Mi Hee | - |
dc.date.accessioned | 2023-12-21T22:44:25Z | - |
dc.date.available | 2023-12-21T22:44:25Z | - |
dc.date.created | 2017-01-19 | - |
dc.date.issued | 2017-01 | - |
dc.description.abstract | Aggregates of amyloidogenic peptides are involved in the pathogenesis of several degenerative disorders. Herein, an iridium(III) complex, Ir-1, is reported as a chemical tool for oxidizing amyloidogenic peptides upon photoactivation and subsequently modulating their aggregation pathways. Ir-1 was rationally designed based on multiple characteristics, including 1)photoproperties leading to excitation by low-energy radiation; 2)generation of reactive oxygen species responsible for peptide oxidation upon photoactivation under mild conditions; and 3)relatively easy incorporation of a ligand on the IrIII center for specific interactions with amyloidogenic peptides. Biochemical and biophysical investigations illuminate that the oxidation of representative amyloidogenic peptides (i.e., amyloid-β, α-synuclein, and human islet amyloid polypeptide) is promoted by light-activated Ir-1, which alters the conformations and aggregation pathways of the peptides. Additionally, their potential oxidation sites are identified as methionine, histidine, or tyrosine residues. Overall, our studies on Ir-1 demonstrate the feasibility of devising metal complexes as chemical tools suitable for elucidating the nature of amyloidogenic peptides at the molecular level, as well as controlling their aggregation. | - |
dc.identifier.bibliographicCitation | CHEMISTRY-A EUROPEAN JOURNAL, v.23, no.7, pp.1645 - 1653 | - |
dc.identifier.doi | 10.1002/chem.201604751 | - |
dc.identifier.issn | 0947-6539 | - |
dc.identifier.scopusid | 2-s2.0-85007552127 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/21330 | - |
dc.identifier.url | http://onlinelibrary.wiley.com/doi/10.1002/chem.201604751/abstract | - |
dc.identifier.wosid | 000395754200024 | - |
dc.language | 영어 | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.title | An Iridium(III) Complex as a Photoactivatable Tool for Oxidation of Amyloidogenic Peptides with Subsequent Modulation of Peptide Aggregation | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | aggregation | - |
dc.subject.keywordAuthor | iridium | - |
dc.subject.keywordAuthor | oxidation | - |
dc.subject.keywordAuthor | peptides | - |
dc.subject.keywordAuthor | photochemistry | - |
dc.subject.keywordPlus | METAL-CATALYZED OXIDATION | - |
dc.subject.keywordPlus | MOBILITY-MASS SPECTROMETRY | - |
dc.subject.keywordPlus | ALPHA-SYNUCLEIN | - |
dc.subject.keywordPlus | CROSS-LINKING | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | BETA-PEPTIDE | - |
dc.subject.keywordPlus | A-BETA | - |
dc.subject.keywordPlus | METHIONINE OXIDATION | - |
dc.subject.keywordPlus | PARKINSONS-DISEASE | - |
dc.subject.keywordPlus | STRUCTURAL-CHARACTERIZATION | - |
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