Methods for analyzing the coordination and aggregation of metal–amyloid-β

Author:

Park Seongmin1ORCID,Na Chanju1ORCID,Han Jiyeon2ORCID,Lim Mi Hee1ORCID

Affiliation:

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

2. Department of Applied Chemistry, University of Seoul , Seoul 02504, Republic of Korea

Abstract

Abstract The misfolding and aggregation of amyloid-β (Aβ) peptides are histopathological features found in the brains of Alzheimer's disease (AD). To discover effective therapeutics for AD, numerous efforts have been made to control the aggregation of Aβ species and their interactions with other pathological factors, including metal ions. Metal ions, such as Cu(II) and Zn(II), can bind to Aβ peptides forming metal-bound Aβ (metal–Aβ) complexes and, subsequently, alter their aggregation pathways. In particular, redox-active metal ions bound to Aβ species can produce reactive oxygen species leading to oxidative stress. In this review, we briefly illustrate some experimental approaches for characterizing the coordination and aggregation properties of metal–Aβ complexes.

Funder

National Research Foundation

Publisher

Oxford University Press (OUP)

Subject

Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)

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