Anand Priya, Nandel Fateh S, Hansmann Ulrich H E
Department of Biophysics, Panjab University, Chandigarh-160014, India.
J Chem Phys. 2008 Nov 21;129(19):195102. doi: 10.1063/1.3021062.
Oligomers of Abeta peptides are suspected as the underlying cause of Alzheimer disease. Knowledge of their structural properties could therefore lead to a deeper understanding of the mechanism behind the outbreak of this disease. As a step in this direction we have studied Abeta dimers by all-atom molecular dynamics simulations. Equilibrated structures at 300 K were clustered into different families with similar structural features. The dominant cluster has parallel N-terminals and a well defined segment Leu17-Ala21 that are stabilized by salt bridges between Lys28 of one chain and either Glu22 or Asp23 of the other chain. The formation of these salt bridges may be the limiting step in oligomerization and fibrillogenesis.
β-淀粉样肽的寡聚体被怀疑是阿尔茨海默病的潜在病因。因此，了解它们的结构特性可能会使人们更深入地理解这种疾病爆发背后的机制。作为朝这个方向迈出的一步，我们通过全原子分子动力学模拟研究了β-淀粉样肽二聚体。300K下的平衡结构被聚类为具有相似结构特征的不同家族。主要的聚类具有平行的N端和一个定义明确的Leu17-Ala21片段，该片段通过一条链的Lys28与另一条链的Glu22或Asp23之间的盐桥得以稳定。这些盐桥的形成可能是寡聚化和纤维形成过程中的限制步骤。
