Studying the helical conformations of aspereline peptides.

Asperelines are short-sequence peptaibol molecules, and these peptides composed of 10 residues were isolated from the Trichoderma asperellum. In our study, a detailed structural characterization was performed on the asperelines by means of molecular dynamics methods. For the aspereline peptides, the occurrence of various secondary structural elements (i.e. β-turns and helical structures) was investigated along their entire sequences. The results derived from the simulated annealing calculations led to the observations that in the case of asperelines, the types I, III and III' β-turn structures, as well as their stabilizing i ← i+3 H-bonds appeared. However, beside the different β-turns, shorter or longer helical structures were also detected. Based on the results obtained by the molecular dynamics simulations, it was concluded that the three-dimensional structure of aspereline peptides could be characterized by helical conformations (i.e. 3 - and α-helix). Nevertheless, on the basis of individual molecular dynamics trajectories, it was observed that the asperelines could adopt not only the right-handed, but also the left-handed helical structures.