Cystine peptides.

Abstract

NHCH 3 (X = Gly 1 , Ala 2 , Aib 3 , Leu 4 and D‐Ala 5 ), have been investigated by Raman and circular dichroism (CD) spectroscopy. Solid state Raman spectra are consistent with β‐turn conformations in all five peptides. These peptides exhibit similar conformations of the disulfide segment in the solid state with a characteristic disulfide stretching frequency at 519 ± 3 cm ‐1 , indicative of a trans‐gauche‐gauche arrangement about the C α —C β —S—S—C β —C α bonds. The results correlate well with the solid state conformations determined by X‐ray diffraction for peptides 3 and 4. CD studies in chloroform and dimethylsulfoxide establish solvent dependent conformational changes for peptides 1, 3 and 5. Disulfide chirality has been derived using the quadrant rule. CD results together with previously reported nuclear magnetic resonance (n.m.r.) data suggest a conformational coupling between the peptide backbone and the disulfide segment.