The dehydropeptide Ac-ΔPhe-l-Val-ΔPhe-NH-Me, containing two dehydrophenylalanine (ΔPhe) residues, crystallizes from methanol/water in space group P212121 with a= 12.622 (1), b= 12.979 (1), and c= 15.733 (1) Å. In the solid state, the molecular structure is characterized by the presence of two intramolecular hydrogen bonds which form two consecutive β-bends. The (φ,Ψ) torsion angles of the three residues are very similar and close to the standard values of type III β-bends, so the molecular conformation corresponds to an incipient right-handed 310 -helix, only slightly distorted. In the crystal, the molecules are linked by head-to-tail hydrogen bonds, thus forming continuous helical columns packed in antiparallel mode. There are no lateral hydrogen bonds; the only interactions are hydrophobic contacts between the apolar side chains of neighboring helical columns

The pentapeptide Boc-Val-delta Phe-Gly-delta Phe-Val-OME, containing two dehydro-phenylalanine (delta Phe) residues, has been synthesized and its structure investigated. In the crystalline state, the molecule adopts a right-handed 3(10)-helical conformation stabilized by two intramolecular hydrogen bonds between CO of Val1 and NH of delta Phe4, and between CO of delta Phe2 and NH of Val5, respectively. NMR measurements are consistent with the presence of 3(10)-helical structures also in acetonitrile and dimethylsulphoxide solution: the distances between backbone protons estimated from NOE connectivities are in overall agreement with those observed in the solid state; the chemical shifts of the amide protons show the smaller temperature coefficients for the NHs that in solid state are involved in intramolecular hydrogen bonds. The CD spectra in acetonitrile, chloroform, methanol and dimethylsulphoxide display exciton couplets of bands corresponding to the delta Phe electronic transition at 280 nm; the sign of the bands is consistent with the presence of helical structures having a prevalent left-handed screw sense. Addition of 1,1,1,3,3,3-hexafluoro-propan-2-ol gives rise to the gradual appearance of a couplet of opposite sign, suggesting the helix reversal from left-handed sense to right-handed sense. The conformational behaviour is discussed on the basis of the specific sequence of the peptide.