Cited 7 time in webofscience Cited 7 time in scopus

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, Ju HyeLee, Shin Jung C.Nam, Jung SeungLee, Hyuck JinKang, Myeong GyunKorshavn, Kyle J.Kim, Hyun TakCho, Jae HeungRamamoorthy, AyyalusamyRhee, Hyun WooKwon, Tae HyukLim, Mi Hee
DGIST Authors
Cho, Jae Heung
Issue Date
2017
Citation
Chemistry - A European Journal, 23(7), 1645-1653
Type
Article
Article Type
Article
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
Related Researcher
  • Author Cho, Jaeheung Biomimetic Materials Laboratory
  • Research Interests Biomimetics; Metalloenzymes; Nitric Oxide Suppliers in Brain; Biomimetic Materials in Life
Files:
There are no files associated with this item.
Collection:
Department of Emerging Materials ScienceBiomimetic Materials Laboratory1. Journal Articles


qrcode mendeley

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE