The Toxic Conformation of the 42-residue Amyloid β Peptide and Its Relevance to Oxidative Stress in Alzheimers Disease

Title: The Toxic Conformation of the 42-residue Amyloid β Peptide and Its Relevance to Oxidative Stress in Alzheimers Disease

Volume: 7 Issue: 10

Author(s): K. Irie, K. Murakami, Y. Masuda, A. Morimoto, H. Ohigashi, H. Hara, R. Ohashi, K. Takegoshi, H. Fukuda, M. Nagao, T. Shimizu and T. Shirasawa

Affiliation:

Keywords: Alzheimer's disease, amyloidβ, cerebral amyloid angiopathy, ESR, neurotoxicity, proline, oxidative stress, solidstate NMR

Abstract: Senile plaques in the brain of patients with Alzheimers disease mainly consist of aggregates of amyloid β peptides (Aβ42, Aβ40). Aβ42 is more neurotoxic than Aβ40. This review describes recent findings from a structural analysis of Aβ42 aggregates and discusses their relevance to neurotoxicity through the formation of radicals.

Cite this article as:

Irie K., Murakami K., Masuda Y., Morimoto A., Ohigashi H., Hara H., Ohashi R., Takegoshi K., Fukuda H., Nagao M., Shimizu T. and Shirasawa T., The Toxic Conformation of the 42-residue Amyloid β Peptide and Its Relevance to Oxidative Stress in Alzheimers Disease, Mini-Reviews in Medicinal Chemistry 2007; 7 (10) . https://dx.doi.org/10.2174/138955707782110187