Kink in Helical Peptides Affects Membrane Pore Formation

Abstract

Antimicrobial peptides (AMPs) can kill pathogenic cells via the formation of membrane pores. However, the connection between peptide properties and their effect on pore formation remains elusive. In particular, the role of proline/glycine kink in helical AMPs has been reported with contradictory effects on antimicrobial activity. Using computer simulations and fluorescence leakage experiments we show the relationship between alpha-helical kink and the structure of the formed pore. Reconciling previous data, the presence of kinks was found to have both stabilizing or destabilizing effect, depending on the pore structure. Moreover, the position of proline/glycine kink in AMP sequence controls the peptide arrangements in the stabilized pores. The provided knowledge can be utilized to rationally design peptides with different ability to form membrane pores useful for the development of new antibacterial agents. To read this article in full you will need to make a payment