New Peptidic Foldamer Structures

化学系的大分子，超分子和纳米化学计划支持塞缪尔·盖尔曼教授的研究，他是威斯康星州-麦迪逊大学化学系的教员。 Gellman的团队基于生物灵感设计开发了新型蛋白质样分子。生物系统包含序列特异性寡聚体和聚合物，它们可以折叠成特定的形状。盖尔曼的实验室创造了非自然的低聚物，或“折叠体”，也采取离散的形状。 这项研究采用β-和γ-氨基酸作为天然α-氨基酸的替代构建块。蛋白质折叠过程将关键的亚基排列成精确的三维阵列，这是与其他分子结合和催化化学反应所必需的。 Gellman小组研究的一个中心目标是开发显示蛋白质样结合和/或催化特性的合成折叠体。 这些材料最终可能在特定功能方面超过蛋白质。 这项基础研究可能会导致新型药物分子或新型纳米级制造能力。 开展这项研究为本科生和研究生提供了出色的跨学科培训。折叠体的研究是化学研究的一个领域，为基础研究和实践发展提供了发明的机会。 这项研究重点关注分子设计方面的前沿挑战。 目的之一是将对小分子构象倾向的理解与从较小分子构建的低聚物中出现的高阶结构偏好联系起来。 特别是，Gellman小组创造了含有β-和/或γ-氨基酸残基的二级结构，这些氨基酸残基形成了具有大内腔的新螺旋二级结构，这是蛋白质二级结构中没有的特征。 第二个目标是利用先前获得的β-肽和α/β-肽折叠行为的知识，以催化合成有用反应的方式排列反应基团对。 第三个目标侧重于定量评估折叠体螺旋的结构稳定性关系，迄今为止基本上无法获得的信息。该研究小组试图了解亚基结构的变化如何影响折叠体二级结构的稳定性。 这些目标的进展可能会提高对分子结构和功能之间关系的理解。

The Macromolecular, Supramolecular and Nanochemistry Program of the Chemistry Division supports the research of Professor Samuel Gellman, who is a faculty member in the Department of Chemistry at the University of Wisconsin - Madison. Gellman's group develops new types of protein-like molecules, based on biologically-inspired designs. Biological systems contain sequence-specific oligomers and polymers that fold to particular shapes. Gellman's laboratory creates unnatural oligomers, or "foldamers", that also adopt discrete shapes. This research employs beta- and gamma-amino acids as alternative building blocks to the natural alpha-amino acids. The protein folding process arranges key subunits into the precise three-dimensional arrays that are necessary for binding to other molecules and catalyzing chemical reactions. A central aim of the Gellman group's research is to develop synthetic foldamers that display protein-like binding and/or catalytic properties. These materials ultimately might surpass proteins in terms of specific functions. This basic research may lead to new types of drug molecules or new types of nanoscale manufacturing capabilities. Conducting this research provides outstanding interdisciplinary training to undergraduates and graduate students.The study of foldamers is an area of chemistry research that offers opportunities for invention in terms of basic research and practical development. This research focuses on cutting-edge challenges in terms of molecular design. One aim is to link understanding of small-molecule conformational propensities to the higher-order structure preferences that emerge in oligomers built from the smaller molecules. In particular, The Gellman group creates secondary structures containing beta- and/or gamma-amino acid residues that form new helical secondary structures with large internal cavities, a feature not found among protein secondary structures. A second aim is to leverage previously acquired knowledge of beta-peptide and alpha/beta-peptide folding behavior to arrange pairs of reactive groups in ways that catalyze synthetically useful reactions. A third aim focuses on quantitative assessment of structure-stability relationships for foldamer helices, information that has been largely unavailable to date. The research group seeks to understand how changes in subunit structure affects the stability of foldamer secondary structures. Progress toward each of these goals may improve understanding of relationships between molecular structure and function.