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

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Chemistry (Weinheim an der Bergstrasse, Germany), ISSN: 1521-3765, Vol: 23, Issue: 7, Page: 1645-1653

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Kang, Juhye; Lee, Shin Jung C; Nam, Jung Seung; Lee, Hyuck Jin; Kang, Myeong-Gyun; Korshavn, Kyle J; Kim, Hyun-Tak; Cho, Jaeheung; Ramamoorthy, Ayyalusamy; Rhee, Hyun-Woo; Kwon, Tae-Hyuk; Lim, Mi Hee Show More Hide
Chemistry; aggregation; iridium; oxidation; peptides; photochemistry
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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 Ir 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.