An Iridium(III) Complex as a Photoactivatable Tool for Oxidation of Amyloidogenic Peptides with Subsequent Modulation of Peptide Aggregation
Cited 0 times inCited 0 times in
- An Iridium(III) Complex as a Photoactivatable Tool for Oxidation of Amyloidogenic Peptides with Subsequent Modulation of Peptide Aggregation
- Kang, Juhye; Lee, Shin Jung C.; Nam. Jung Seung; Lee, Hyuck Jin; Kang, Mueong-G.; Korshavn, Kyle J.; Kim, Hyun-Tak; Cho, Jaeheung; Ramamoorthy, Ayyalusamy; Rhee, Hyun-Woo; Kwon, Tae-Hyuk; Lim, Mi Hee
- aggregation; iridium; oxidation; peptides; photochemistry
- Issue Date
- WILEY-V C H VERLAG GMBH
- CHEMISTRY-A EUROPEAN JOURNAL, v.23, no.7, pp.1645 - 1653
- 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.
- ; Go to Link
Appears in Collections:
- SNS_Journal Papers
can give you direct access to the published full text of this article. (UNISTARs only)
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.