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Time-Dependent DNA Condensation Induced by Amyloid ß-Peptide

Division of Biological Inorganic Chemistry, Key Laboratory of Rare Earth Chemistry and Physics, Changchun Institute of Applied Chemistry, Graduate School of the Chinese Academy of Sciences, Changchun, Jilin, China

Correspondence: Address reprint requests to Xiaogang Qu, Division of Biological Inorganic Chemistry, Key Laboratory of Rare Earth Chemistry and Physics, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, China. Tel.: 86-431-526-2656; Fax: 86-431-5262656; E-mail: xqu{at}ciac.jl.cn.

The major protein component of the amyloid deposition in Alzheimer's disease is a 39–43 residue peptide, amyloid ß (Aß). Aß is toxic to neurons, although the mechanism of neurodegeneration is uncertain. Evidence exists for non-B DNA conformation in the hippocampus of Alzheimer's disease brains, and Aß was reportedly able to transform DNA conformation in vitro. In this study, we found that DNA conformation was altered in the presence of Aß, and Aß induced DNA condensation in a time-dependent manner. Furthermore, Aß sheets, serving as condensation nuclei, were crucial for DNA condensation, and Cu²⁺ and Zn²⁺ ions inhibited Aß sheet-induced DNA condensation. Our results suggest DNA condensation as a mechanism of Aß toxicity.