A? PEPTIDES INTERACTIONS WITH LIPID BILAYERS: IMPLICATIONS FOR AGGREGATION AND

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 淀粉样蛋白-？(a？)多肽具有很强的膜结合能力，可通过改变膜的完整性和通透性而对神经元产生细胞毒作用。然而，A？神经毒性，即这些多肽是否形成离子通道/孔或引起膜缺陷，目前尚不清楚。通过比较低聚物结构的两种状态(溶液和膜上)和两种膜破坏机制(膜完整性和离子通道)，建立了从水到膜环境的低聚物结构转变与细胞膜生物活性之间的分子水平关系。具有明显结构形态的低聚物。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Amyloid-? (A?) peptides have a strong membrane-associated ability that can induce cytotoxicity to neurons by altering membrane integrity and permeability. However, the molecular mechanism underlying A? neurotoxicity, i.e. whether these peptides form ion channels/pores or induce membrane defects, remains unclear. The proposed work strives to establish a molecular-level relationship between oligomer structural transition from the aqueous to the membrane environment and their biological activity in cell membranes by comparing two states of oligomer structures (in solution vs. on membrane) and two types of membrane disruption mechanism (membrane integrity vs. ion-channel) for different A? oligomers with distinct structural morphology.