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中文摘要：
离子 amyloidbeta 肽(贝它) 的 oligomers 的像隧道的 nanotube 结构被分子的建模首先调查。结果表明氢键网是关键因素之一稳定结构。支链的 hydrophobicitydistribution 模式赞成插入到双性人层并且形成一个吸水的毛孔的结构。腔空格连续地在否定潜力的控制下面、更弱却散布，到哪个阳离子选择属性；同时，更强壮的积极、否定的潜力的交替的分发做结构框架平衡的静电的分发，它也是稳定结构的关键因素之一。结果为照亮结构稳定性和离子渗透打了理论基础，并且把线索给阐明 Alzheimer 的疾病(广告) 和设计小说的分子的机制在根阻止或逆行广告的药。
英文摘要：
The ion channel-like nanotube structure of the oligomers of amyloid β-peptide （Aβ） was first investigated by molecular modeling. The results reveal that the hydrogen bond net is one of the key factors to stabilize the structure. The hydrophobicity distribution mode of the side chains is in favor of the structure inserting into the bilayers and forming a hydrophilic pore. The lumen space is under the control of the negative potential, weaker but spreading continuously, to which the cation selectivity attributes; meanwhile, the alternate distribution of the stronger positive and negative potentials makes the electrostatic distribution of the structure framework balance, which is also one of the key factors stabilizing the structure. The results lay the theoretical foundation for illuminating the structure stability and the ion permeability, and give a clue to elucidating the molecular mechanism of Alzheimer＇s disease （AD） and designing novel drugs to prevent or reverse AD at the root.
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