Consecutive cyclic pentapeptide modules form short alpha-helices that are very stable to water and denaturants.

A generic approach to mimicking α-helices has been achieved by using sequences of consecutive macrocyclic pentapeptides (for example, cyclo(1 → 5)-Ac-[KARAD] -NH ) to form 3-turn (see picture) and 4-turn α-helices, which have high conformational stability in water and are resistant to protein-denaturing conditions (65 °C, 8 M guanidine·HCl, trypsin digestion).