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.
