A series of tetrapeptide amides containing two aminoisobutyric acids (Aib) and two -methylphenylalanine ((Me)Phe) units were prepared through the 'azirine/oxazolone method'. New 2-benzyl-2-methyl-2Hazirin-3-amines have been used for the selective introduction of (S)-and (R)-(Me)Phe, respectively. The solid-state conformations of five tetrapeptide amides were determined by X-ray crystallography. In all cases, two -turns stabilize 310-helical conformations and it was confirmed that, in contrast to proteinogenic amino acids, the configuration of (Me)Phe does not determine the screw sense of the helix.