【摘 要】
：
Aβ25-35,a proteolytic fragment of the Alzheimer amyloid beta (Aβ) peptide,retains the neurotoxicity of its full-length counterpart.The formation of pores/channels in membranes has been reported as one
【机 构】
：
复旦大学物理系和应用表面物理国家重点实验室
【出 处】
：
中国物理学会2011年秋季学术会议
论文部分内容阅读
Aβ25-35,a proteolytic fragment of the Alzheimer amyloid beta (Aβ) peptide,retains the neurotoxicity of its full-length counterpart.The formation of pores/channels in membranes has been reported as one of the mechanism responsible for Aβ25-35 toxicity and the pore/channel structure was thought to be formed by the aggregation of Aβ25-35 in membranes into a β-barrel structure.However,the structure of β-barrel and its perturbation on the ordering of lipid bilayer at atomic level remain elusive.
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