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Kwon, Tae-Hyuk
Energy Recognition
Research Interests
  • Energy transfer, organic solar cells, supercapacitor, ultrasonic spray chemistry, dithienothiophene, iridium complexes, phosphorescent bioapplications

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

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Title
An Iridium(III) Complex as a Photoactivatable Tool for Oxidation of Amyloidogenic Peptides with Subsequent Modulation of Peptide Aggregation
Author
Kang, JuhyeLee, Shin Jung C.Nam. Jung SeungLee, Hyuck JinKang, Mueong-G.Korshavn, Kyle J.Kim, Hyun-TakCho, JaeheungRamamoorthy, AyyalusamyRhee, Hyun-WooKwon, Tae-HyukLim, Mi Hee
Keywords
aggregation; iridium; oxidation; peptides; photochemistry
Issue Date
201701
Publisher
WILEY-V C H VERLAG GMBH
Citation
CHEMISTRY-A EUROPEAN JOURNAL, v.23, no.7, pp.1645 - 1653
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.
URI
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DOI
http://dx.doi.org/10.1002/chem.201604751
ISSN
0947-6539
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