Minimalistic amino amides as models to study N–H⋯π interactions and their implication in the side chain folding of pseudopeptidic molecules

Abstract

The structural study of simple amino amides derived from natural amino acids showed a unique conformational pattern for the aromatic residues, being clearly different from that for the aliphatic derivatives. The results from a detailed NMR analysis, supported by DFT calculations, indicate that the aromatic side chain tends to fold over the amino amide moiety, involving a stabilizing polar N–H⋯π interaction. The implications of this folding in the establishing of non-covalent interactions is also discussed.