Effects of Zinc Binding on the Conformational Distribution of the Amyloid-β Peptide Based on Molecular Dynamics Simulations

• DOI: 10.1021/jp076213t
• Publication Date: 2007-11-15T10:01:02Z
• Authors: Wenfei Li; Jian Zhang; Yu Su; Jun Wang; Meng Qin; Wei Wang
• Keywords: Amyloid beta; Peptide Conformation; Amyloid (mycology); Conformational change; P3 peptide

A number of experiments suggested that metal binding can promote the aggregation amyloid-β peptide. In this work, effects zinc on conformational distributions full length peptide are investigated basis extensive molecular dynamics simulations. By comparing apo-peptide and holo-peptide, we show affect distribution monomer dramatically. Compared with apo-peptide, holo-peptide samples more β-strand conformation for central hydrophobic cluster 17−21. Meanwhile, formation probabilities salt bridge Asp23−Lys28 turn comprising 23−28 also increased significantly at room temperature. Since these local structures essential aggregation, observed indicate induced change is one possible mechanisms promoted