Synthesis of Ion Channel Forming Peptides

在本科院校研究奖的支持下， 有机合成计划和多学科办公室 数学和物理科学理事会的活动， Karin S.罗格斯大学化学系的Akerfeldt说， 新泽西的州立大学，卡姆登校区，进行 离子通道形成肽的合成和分析。 结构上 合成了定义明确的人工质子选择性通道， 模型来研究质子运输的基本机制。 该模型被设计成形成两亲性α螺旋， 膜并且在施加电场的存在下， 自缔合以形成导电螺旋束。 以下设计 合适的肽序列，以允许方便的处理，共价地 制备设计序列的连接二聚体以探测因子 影响通道稳定性，同时掺入正缬氨酸 衍生到序列的特定位置允许评估 它们对肽的堆积特性的影响。 允许离子或小分子运输的膜通道， 构成了跨细胞通信的关键模式之一 膜。 此外，它们在细胞调节和介导 神经和肌肉系统的所有电兴奋性。 教授 卡琳·S美国罗格斯大学化学系的Akerfeldt说， 新泽西大学卡姆登校区，在一项研究的支持下， 在本科院校奖从有机合成计划 和数学和科学研究所多学科活动办公室 物理科学理事会，准备相对较小的模型 设计用作跨膜离子通道的多肽。 通过 这些模型化合物的合成和研究， 探讨了影响离子跨膜流动的各种因素。 这些因素很难用自然发生的 通道形成肽由于其复杂性， 缺乏膜，并且在显著的情况下通常可用性有限， 是介于

With the support of a Research in Undergraduate Institutions award from the Organic Synthesis Program and the Office of Multidisciplinary Activities of the Mathematical and Physical Sciences Directorate, Professor Karin S. Akerfeldt, of the Department of Chemistry at Rutgers, the State University of New Jersey, Camden Campus, carries out the synthesis and analysis of ion channel forming peptides. Structurally well-defined artificial proton selective channels are synthesized as models to study the fundamental mechanisms involved in proton transport. The models are designed to form amphiphilic alpha helices which, in a membrane and in the presence of an applied electrical field, self-associate to form conducting helix bundles. Following design of suitable peptide sequences to allow convenient handling, covalently linked dimers of the designed sequences are prepared to probe the factors influencing channel stability, while incorporation of norvaline derivatives into specific positions of the sequences permits evaluation of their effects on the packing properties of the peptides. Membrane channels, permitting the transport of ions or small molecules, constitute one of the critical modes of communication across cell membranes. In addition, they are critical in cell regulation and mediate all electrical excitability of the nervous and muscle systems. Professor Karin S. Akerfeldt, of the Department of Chemistry at Rutgers, the State University of New Jersey, Camden Campus, with the support of a Research in Undergraduate Institutions award from the Organic Synthesis Program and the Office of Multidisciplinary Activities of the Mathematical and Physical Sciences Directorate, prepares comparatively small model polypeptides designed to serve as transmembrane ion channels. Through the synthesis and study of these model compounds, Professor Akerfeldt explores various factors influencing the flow of ions across membranes. These factors are difficult to explore with the naturally occurring channel-forming peptides given their complexity, instability in the absence of membranes, and often limited availability in significant quantities.