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Unveiling the impact of oxidation-driven endogenous protein interactions on the dynamics of amyloid-beta aggregation and toxicity

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Title
Unveiling the impact of oxidation-driven endogenous protein interactions on the dynamics of amyloid-beta aggregation and toxicity
Author(s)
Du, Zhi; Nam, Eunju; Lin, Yuxi; Mannkyu Hong; Molnar, Tamas; Kondo, Ikufumi; Ishimori, Koichiro; Mu-Hyun Baik; Lee, Young-Ho; Lim, Mi Hee
Publication Date
2023-05
Journal
Chemical Science, v.14, no.20, pp.5340 - 5349
Publisher
Royal Society of Chemistry
Abstract
Cytochrome c (Cyt c), a multifunctional protein with a crucial role in controlling cell fate, has been implicated in the amyloid pathology associated with Alzheimer's disease (AD); however, the interaction between Cyt c and amyloid-beta (A beta) with the consequent impact on the aggregation and toxicity of A beta is not known. Here we report that Cyt c can directly bind to A beta and alter the aggregation and toxicity profiles of A beta in a manner that is dependent on the presence of a peroxide. When combined with hydrogen peroxide (H2O2), Cyt c redirects A beta peptides into less toxic, off-pathway amorphous aggregates, whereas without H2O2, it promotes A beta fibrillization. The mechanisms behind these effects may involve a combination of the complexation between Cyt c and A beta, the oxidation of A beta by Cyt c and H2O2, and the modification of Cyt c by H2O2. Our findings demonstrate a new function of Cyt c as a modulator against A beta amyloidogenesis.
URI
https://pr.ibs.re.kr/handle/8788114/13687
DOI
10.1039/d3sc00881a
ISSN
2041-6520
Appears in Collections:
Center for Catalytic Hydrocarbon Functionalizations(분자활성 촉매반응 연구단) > 1. Journal Papers (저널논문)
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