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

Author:

Du Zhi12,Nam Eunju1,Lin Yuxi3,Hong Mannkyu14,Molnár Tamás5,Kondo Ikufumi6,Ishimori Koichiro67ORCID,Baik Mu-Hyun14ORCID,Lee Young-Ho38910,Lim Mi Hee1ORCID

Affiliation:

1. Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea

2. Department of Biomedical Engineering, College of Biomedical Engineering, Taiyuan University of Technology, Taiyuan 030024, PR China

3. Research Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Ochang, Chungbuk 28119, Republic of Korea

4. Center for Catalytic Hydrocarbon Functionalizations, Institute for Basic Science (IBS), Daejeon 34141, Republic of Korea

5. Department of Biochemistry, Institute of Biology, Eötvös Loránd University, H-1117 Budapest, Hungary

6. Graduate School of Chemical Sciences and Engineering, Hokkaido University, Kita 13, Nishi 8, Kita-ku, Sapporo 060-8628, Japan

7. Department of Chemistry, Faculty of Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo 060-0810, Japan

8. Bio-Analytical Science, University of Science and Technology (UST), Daejeon 34113, Republic of Korea

9. Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134, Republic of Korea

10. Research Headquarters, Korea Brain Research Institute (KBRI), Daegu 41068, Republic of Korea

Abstract

We illuminate that cytochrome c (Cyt c) directly interacts with amyloid-β (Aβ) and alters Aβ amyloidogenesis in a peroxide-dependent manner, which demonstrates its new role towards the amyloid pathology associated with Alzheimer's disease.

Funder

Institute for Basic Science

National Research Foundation of Korea

National Research Council of Science and Technology

Korea Basic Science Institute

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

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