A New Class of Foldamers Based oncis-γ-Amino-l-proline1,2

Abstract
A synthetic method for the preparation of conformationally constrained γ-peptides derived from γ-amino-l-proline is described. The methodology allows the independent buildup of the peptide backbone and the introduction of sequential variations by reactions with the α-amino group of γ-aminoproline. Both alkyl- and acyl-substituted γ-peptides have been prepared and studied by CD and NMR. Conformational restrictions due to the cyclic structure of the monomer give rise to long-range interactions that are indicative of secondary structures even in aqueous solution. Interresidue NOEs suggest a concatenation of turns that, in a permissive solvent, could give rise to an isolated hydrogen bond ribbon, flanked and protected by proline rings.

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