Mini-protein scaffolds for protein design

该研究计划的重点是实施互补设计和筛选工具，用于开发具有确定结构和化学计量的微型蛋白质基序。新的溶剂化显色氨基酸将被设计和合成，然后整合到测试肽和评估，以评估其效用作为探针研究蛋白质-蛋白质相互作用在合成和天然系统。将开发完全由编码的氨基酸组成的迷你蛋白基序，增加了生物而不是化学系统可以用于从表达文库中产生和选择有用基序的可能性。后者的研究将专门针对卟啉结合的微型蛋白基序的发展。有机和大分子化学计划正在支持马萨诸塞州理工学院化学系的Barbara Imperiali教授的研究。蛋白质（多肽）由相互连接的氨基酸长链组成，发挥着无数的生物化学作用。它们的特定功能严重依赖于多肽链所采用的三维结构，但负责蛋白质折叠的因素仍然不完全了解。通过设计，合成和小多肽的研究，Imperiali教授正在阐明负责形成特定蛋白质折叠基序的因素。她的研究还探索了这些“迷你图案”可以作为支架来识别和感知小有机分子的可能性。

This research program is focused on implementing complementary design and screening tools for the development of mini-protein motifs of defined structure and stoichiometry. New solvatochromic amino acids will be designed and synthesized, then integrated into test peptides and evaluated to assess their utility as probes for investigating protein-protein interactions in synthetic and natural systems. Mini-protein motifs comprised entirely of the encoded amino acids will be developed, increasing the likelihood that biological rather than chemical systems could be exploited for the generation and selection of useful motifs from expressed libraries. The latter studies will specifically target the development of a porphyrin-binding mini-protein motif.The Organic and Macromolecular Chemistry Program is supporting the research of Professor Barbara Imperiali, of the Department of Chemistry at the Massachusetts Institute of Technology. Proteins (polypeptides), comprised of long chains of interconnected amino acids, play myriad biochemical roles. Their specific function is critically dependent on the three dimensional structure adopted by the polypeptide chain, yet the factors responsible for protein folding are still at best incompletely understood. Through the design, synthesis, and study of small polypeptides, Professor Imperiali is shedding light on the factors responsible for the formation of particular protein folding motifs. Her studies also explore the possibility that these "mini-motifs" could serve as scaffolds to permit the recognition and sensing of small organic molecules.