Minimalistic amino amides as models to study N–Hπ 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–Hπ interaction. The implications of this folding in the establishing of non-covalent interactions is also discussed.