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An Iridium(III) Complex as a Photoactivatable Tool for Oxidation of Amyloidogenic Peptides with Subsequent Modulation of Peptide Aggregation

Title
An Iridium(III) Complex as a Photoactivatable Tool for Oxidation of Amyloidogenic Peptides with Subsequent Modulation of Peptide Aggregation
Authors
Kang, J.[Kang, Ju Hye]Lee, S.J.C.[Lee, Shin Jung C.]Nam, J.S.[Nam, Jung Seung]Lee, H.J.[Lee, Hyuck Jin]Kang, M.-G.[Kang, Myeong Gyun]Korshavn, K.J.[Korshavn, Kyle J.]Kim, H.-T.[Kim, Hyun Tak]Cho, J.[Cho, Jae Heung]Ramamoorthy, A.[Ramamoorthy, Ayyalusamy]Rhee, H.-W.[Rhee, Hyun Woo]Kwon, T.-H.[Kwon, Tae Hyuk]Lim, M.H.[Lim, Mi Hee]
DGIST Authors
Cho, J.[Cho, Jae Heung]
Issue Date
2017
Citation
Chemistry - A European Journal, 23(7), 1645-1653
Type
Article
Article Type
Article in Press
Keywords
AgglomerationAggregationAmino AcidsAmyloidogenic PeptidesGlycoproteinsIridiumIridium CompoundsLow-Energy RadiationMetal ComplexesMultiple CharacteristicsOxidationPeptide AggregationPeptide OxidationPeptidesPhoto ActivationsPhotochemical ReactionsPhotochemistryProteinsReactive Oxygen Species (ROS)Specific Interaction
ISSN
0947-6539
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. © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
URI
http://hdl.handle.net/20.500.11750/2074
DOI
10.1002/chem.201604751
Publisher
Wiley-VCH Verlag
Files:
There are no files associated with this item.
Collection:
Emerging Materials ScienceETC1. Journal Articles


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