DPI实时探索Aβ_(1-42)和Lilrb2 receptor相互作用的动力学机制
详细信息 查看官网全文
- 英文论文题名：Reveal the real time binding mechanisms between Aβ_(1-42) types and Lilrb2 receptor by Dual Polarization Interferometry
- 论文作者：胡涛 ; 黄光明 ; 杨秀荣
- 英文论文作者：Tao Hu ; Guangming Huang ; Xiurong Yang ; State Key Lab of Electroanalytical Chemistry ; Changchun Institute of Applied Chemistry ; Department of Chemistry ; University of Science and Technology of China
- 年：2016
- 作者机构：中国科学院长春应用化学研究所电分析化学国家重点实验室;中国科学技术大学化学系;
- 论文关键词：阿尔兹海默症 ; Aβ_(1-42)聚集体 ; lilrb2受体 ; 动力学信息
- 会议召开时间：2016-07-01
- 会议录名称：中国化学会第30届学术年会摘要集-第二十八分会：化学生物学
- 语种：中文
- 分类号：R749.16
- 学会代码：ZGHY
- 会议名称：中国化学会第30届学术年会-第二十八分会 ; 化学生物学
- 会议地点：中国辽宁大连
- 主办单位：中国化学会
- 学会名称：中国化学会
- 页数：1
- 文件大小：309k
- 原文格式：D
- 会议级别：全国
摘要
阿尔兹海默症中存在的Aβ_(1-42)聚集体能够引发突触损失与神经细胞死亡。但是,为什么不同类型的Aβ聚集体会导致不同的神经毒性效应还有待探索。这里,我们利用新颖的DPI技术探索Aβ_(1-42)聚集体和lilrb2受体相互作用的动力学机制~([1])。DPI提供的实时结合的动力学信息(解离速率,结合速率)能够间接的解释不同分子质量的Aβ_(1-42)聚集体所导致的不同毒性效应。我们的工作对于研究其他的受体蛋白与不同类型的Aβ_(1-42)聚集体间的相互作用动力学特性提供了新思路,希望本工作对于未来药物的发现和筛选提供指导性的帮助。
The toxic Aβ oligomers types that are found in Alzheimer's disease(AD) seem to cause synaptic loss and neuronal cell death.However,a basic question that why different types of Aβ oligomers exert differential neurotoxicity through binding to receptors remains to be definitively answered.Herein,we introduce a powerful and novel dual polarization interferometry(DPI) technique to explore the interaction between oligomers Aβ_(1-42) and leukocyte immunoglobulin-like receptor B2(lilrb2).The precise analysis of association rate(k_(on)) and dissociation rate(k_(off))based on DPI provides robust information about real-time structural data of their binding events and could indirectly elucidate different malicious impacts trigged by various Aβ oligomers.Strikingly,our study offers a new exciting clue to explore the dynamic properties associated with interactions of oligomers Aβ_(1-42) with other targets and hopefully contributes to drug discovery and screen in future.
The toxic Aβ oligomers types that are found in Alzheimer's disease(AD) seem to cause synaptic loss and neuronal cell death.However,a basic question that why different types of Aβ oligomers exert differential neurotoxicity through binding to receptors remains to be definitively answered.Herein,we introduce a powerful and novel dual polarization interferometry(DPI) technique to explore the interaction between oligomers Aβ_(1-42) and leukocyte immunoglobulin-like receptor B2(lilrb2).The precise analysis of association rate(k_(on)) and dissociation rate(k_(off))based on DPI provides robust information about real-time structural data of their binding events and could indirectly elucidate different malicious impacts trigged by various Aβ oligomers.Strikingly,our study offers a new exciting clue to explore the dynamic properties associated with interactions of oligomers Aβ_(1-42) with other targets and hopefully contributes to drug discovery and screen in future.
引文
[1]Kim,T.;Vidal,G.;William,C.;Birnbaum,M.;Garcia,K.;Hyman,B.;Shatz,C.J.Science.2013,341:1399.