Design of Reaction Catalysts Based on Protein Cavities

有了这个更新奖，有机和高分子化学计划 是继续支持马克Distefano博士在大学 明尼苏达州-双子城。 工作目标是：（1）提高 基于氨基转移催化剂的活性和对映选择性 突变体FABPs（脂肪酸结合蛋白）的蛋白质腔，2） 评估辅因子结构的影响，3）扩大反应范围 包括C-C键形成，4）开发制备和快速筛选催化剂候选物的方法，以及5）开发噬菌体展示 选择可结合吡哆胺类似物的蛋白质空腔的系统 非共价键。 Distefano博士正在开发一系列新的半合成酶样 基于一类蛋白质（FABPs）的催化剂， 空的中心腔，其可用于保持有机基板， 它们是由化学上连接到 蛋白 FABPs易于克隆和高效表达， 允许它们的尺寸和组成具有相当大的可变性。 等 催化剂在制备各种各样的 特种化学品 因为它们在温和的环境下工作 条件下，并由生物降解材料制备，它们也 环境吸引力。

With this Renewal award, the Organic and Macromolecular Chemistry Program is continuing support for Dr. Mark Distefano at the University of Minnesota - Twin Cities. The objectives of the work are to: 1) improve the activities and enantioselectivities of transaminating catalysts based on protein cavities of mutant FABPs (Fatty Acid Binding Proteins), 2) assess the effects of cofactor structure, 3) expand the scope of reaction types to include C-C bond formation, 4) develop methods to prepare and screen rapidly catalyst candidates, and 5) develop a phage display system to select protein cavities that can bind pyridoxamine analogues noncovalently. Dr. Distefano is developing a series of novel semisynthetic enzyme-like catalysts based on a class of proteins (FABPs) that contain a large empty central cavity, which can be used to hold organic substrates while they are operated on by cofactors that are chemically linked to the protein. The FABPs can be easily cloned and efficiently expressed, allowing considerable variability in their size and composition. Such catalysts could be very useful in the preparation of a wide variety of specialty chemicals. Because they operate in water under mild conditions and are prepared from biodegradable materials, they are also environmentally attractive.