CAREER: Metal-Binding Studies of Phosphorylated a-Synuclein Peptides

无机，生物无机和有机化学计划的职业奖支持杜克大学的凯瑟琳J. Franz教授的工作，以探索金属离子对α-突触核蛋白构象的影响，α-突触核蛋白是路易体的主要蛋白质组分，是帕金森病的症状。 荧光技术将用于监测与磷酸化和未磷酸化的α-突触核蛋白相关的合成肽的金属结合。 聚集成原纤维是α-突触核蛋白的特征，并且在研究不聚集的易处理的合成肽之后，该方法将扩展到α-突触核蛋白的原纤维倾向的肽区段。 专业发展所需的重要技能将通过研究生讲习班得到加强。 领导力和沟通将突出在车间设置，职业战略和演示技术将作为研究生专业发展的重要课题。 杜克大学正在参与卡内基博士计划，为研究生计划的专业讲习班的教育目标与重新评估哲学指导博士课程的努力建设性地融合在一起。了解金属离子在蛋白质构象偏好和聚集过程中的作用是一个重要的目标，与修改生物系统密切相关。 对与α突触核蛋白相关的多肽的研究将提供对金属与沿着氨基酸序列的潜在金属结合位点的相互作用的深入了解。

This CAREER award in the Inorganic, Bioinorganic and Organometallic Chemistry program supports work by Professor Katherine J. Franz at Duke University to explore the impact of metal ions on the conformation of a-synuclein, the major protein component of Lewy Bodies, a symptom of Parkinson's Disease. Fluorescence techniques will be used to monitor metal binding to synthetic peptides relevant to both phosphorylated and unphosphorylated a-synuclein. Aggregation into fibrils is characteristic of a-synuclein, and after investigating tractable synthetic peptides which do not aggregate the methodology will be extended to fibril-prone peptide segments of a-synuclein. Important skills necessary for professional development will be enhanced through workshops for graduate students. Leadership and communication will be highlighted in the workshop settings, and career strategies and presentation techniques will be addressed as important topics for graduate student professional development. Duke is participating in the Carnegie Initiative on the Doctorate, and the educational objectives of the professional workshops planned for graduate students merge constructively with efforts to reassess the philosophy guiding PhD curricula in the department.Understanding the role of metal ions in protein conformational preferences and in aggregation processes is an important goal that is germane to modifying biological systems. Studies of polypeptides related to alpha synuclein will provide insight into the interactions of metals with potential metal binding sites along the amino acid sequence.