Investigations of strand-forming foldamers. I. Study of antiparallel and parallel beta-peptide sheet model systems. II. Efforts toward the design of sulfonamide strand mimics.

摘要

The term “foldamer” refers to any monodisperse oligomer that adopts a compact and defined conformation. This dissertation describes the design, synthesis, and study of antiparallel and parallel β-peptide hairpin foldamers. The antiparallel sheet model systems are well-folded in methanol, but not in water. Parallel β-peptide sheet structure was observed in methanol and in the solid state. This dissertation also describes a series of hairpins that were designed to evaluate the ability of sulfonamide groups to serve as one-sided hydrogen bonding complements to α-amino acid residues. A hairpin containing a single sulfonamide group and a single α-amino acid residue displayed the desired one-sided hydrogen bonding interaction. Longer hairpins, containing multiple sulfonamides and α-amino acids, did not display the desired interactions.