Related Experiment Video
Updated: Jul 13, 2026

Modeling Amyloid-β42 Toxicity and Neurodegeneration in Adult Zebrafish Brain
Published on: October 25, 2017
Molecular modeling of zinc and copper binding with Alzheimer's amyloid beta-peptide
Daxiong Han1, Haiyan Wang, Pin Yang
1Department of Pharmacy, Medical College of Xiamen University, Xiamen, China. daxiong@xmu.edu.cn
Abstract:
Aggregation of the amyloid beta-peptide (Abeta) into insoluble fibrils is a key pathological event in Alzheimer's disease. Cu(II) and Zn(II) ions were reported to be able to induce Abeta aggregation at nearly physiological concentrations in vitro. In this study, the binding modes of Cu(II) and Zn(II) in this process were explored by molecular modeling. In the pre-associated Abeta, Ntau atom of imidazole ring of His14, O atom of carbonyl of main-chain and two O atoms of water occupied the four ligand positions of the complex. While in the aggregated form of Abeta, the His13(N)-Metals-His14(N) bridges were formed through metal cross-linking action. These results would be helpful to put insight on revealing the formation mechanism of pathogenic Abeta aggregates in brain.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Alzheimer Disease ll: Pathophysiology
