This grant from the Organic Dynamics Program supports the work of Professor James S. Nowick at the University of California Irvine. A new strategy will be developed for controlling peptide secondary structure by linking multiple amino acid chains to a stiff oligomeric backbone that serves as a molecular scaffold. The molecular scaffold will be based upon an oligourea that will be synthesized in an iterative fashion. This strategy will be used to create beta-sheets and to develop molecular receptors for small peptides. %%% The three dimensional structure of a peptide will be controlled by linking the peptide chain to a rigid molecular backbone. The backbone will be designed to hold several peptides in parallel and antiparallel fashions. This represents a fundamentally new approach to the control of protein structure. The design of the backbone is ideally suited for the development of receptors for small peptides.
