• α-aminoisobutyryl peptides;
  • circular dichroism;
  • peptide conformation;
  • proline peptides;
  • β-turns

The circular dichroism spectra of four β-turn model peptides, Z-Aib-Pro-Aib-Pro-OMe (1), Piv-Pro-Aib-NHMe (2), Piv-Pro-D-Ala-NHMe (3) and Piv-Pro-Val-NHMe (4) have been examined under a wide range of solvent conditions, using methanol, hexafluoroisopropanol and cyclohexane. Type I and Type II β-turns have been observed for peptides 1 and 2 respectively, in the solid state, while the Pro-D-Ala sequence adopts a Type II β-turn in a related peptide crystal structure. A class C spectrum is observed for 1 in various solvents, suggesting a variant of a Type I (III) structure. The Type II β-turn is characterized by a CD spectrum having two positive CD bands at ˜ 230 nm and ˜ 202 nm, a feature observed in Piv-Pro-D-Ala-NHMe in cyclohexane and methanol and for Piv-Pro-Aib-NHMe in methanol. Peptide 2 exhibits solvent dependent CD spectra, which may be rationalized by considering Type II, III and V reverse turn structures. Piv-Pro-Val-NHMe adopts non-β-turn structures in polar solvents, but exhibits a class B spectrum in cyclohexane suggesting a population of Type I β-turns.