Preferred conformations of peptides containing α,α‐disubstituted α‐amino acids

Abstract

Abstract The conformational preferences of linear peptides containing α,α‐disubstituted α‐amino acids, derived from the crystal structures of 28 compounds, are reviewed. In particular, the sensitivity of peptide conformation to the geometry of these unusual amino acids is underlined. We also consider possible future directions of research, which, we hope, will result in a complete understanding of the structures adopted by peptaibol antibiotics.