RUI: Probing Early Events in Amyloid-beta Association by Single-Pair Forster Resonance Energy Transfer

在这个由化学系实验物理化学项目资助的项目中，Robin Lammi和Winthrop大学的本科生研究人员将研究淀粉样蛋白二聚体的结构异质性。肽(第一部;# 946)。这种蛋白质的小聚物与阿尔茨海默病的神经变性密切相关。它可能在有序原纤维生长过程中起到关键的细胞核作用，这些原纤维被用作纳米线和传感器。通过对数十个局部荧光标记的二聚体进行单对Förster共振能量转移（spFRET）测量，一次一个，Lammi和她的学生将直接探测在体溶液测量中模糊的低聚物到低聚物的变化，获得独特的，分子水平的持久性与瞬态二聚体结构的见解。除了提供关于早期阶段的新的实证见解之外；该项目将允许对本科研究人员进行密集的跨学科培训。在本科课程中纳入单低聚物实验室实验，并引入项目衍生数据和分析技术，将先进的研究方法带入课堂，影响Winthrop的所有化学专业，包括许多来自代表性不足群体的学生。

In this project, funded by the Experimental Physical Chemistry Program of the Division of Chemistry, Robin Lammi and undergraduate researchers at Winthrop University will investigate structural heterogeneity in dimers of amyloid-β peptide (Aβ). Small oligomers of this protein are closely linked to neurodegeneration in Alzheimer?s disease and likely serve as critical nuclei in the growth of ordered fibrils used as nanowires and sensors. By performing single-pair Förster resonance energy transfer (spFRET) measurements on dozens of localized, fluorescently labeled dimers, one at a time, Lammi and her students will directly probe the oligomer-to-oligomer variation obscured in bulk-solution measurements, gaining unique, molecular-level insight into persistent versus transient dimer structures. In addition to affording new empirical insights into the earliest steps in Aβ association, this project will permit intense, interdisciplinary training of undergraduate researchers. The inclusion of a single-oligomer laboratory experiment and the introduction of project-derived data and analysis techniques in the undergraduate curriculum will bring advanced research methods into the classroom, impacting all chemistry majors at Winthrop, including many students from underrepresented groups.