Stereospecific Synthesis of Conformationally Constrained γ-Amino Acids: New Foldamer Building Blocks That Support Helical Secondary Structure

摘要

Oligomers constructed from β-amino acid residues ("β-peptides") or from combinations of α- and β-amino acid residues ("α/β-peptides") can adopt protein-like folding patterns.1'2 These con-formational properties provide a basis for the ongoing development of β- and α/β-peptides that display interesting functional properties. β-Amino acid residues can be endowed with higher intrinsic folding propensities than those of α residues by use of cyclic constraints to limit backbone torsional mobility, and this capacity for residue-based rigidification has proven to be important for both the structure and function of β- and α/β-peptide foldamers.