Molecular dynamics simulations were used to investigate spatial structure of antimicrobial peptide buforin 2 in water and in toroidal transmembrane pores. It is shown that Pro11-Ala11 amino acid substitution contributes to stabilization of the helix and enables the peptide to form stable transmembrane toroidal pore. The results obtained correlate with the changes observed when modified buforin 2 interacts with cells.

Molecular dynamics simulations were used to investigate the spatial structure of antimicrobial peptide buforin 2 in water and in toroidal transmembrane pores. It is shown that replacement of Pro11 with Ala straightens and stabilizes the helix and enables the peptide to form a stable transmembrane toroidal pore. The results obtained correlate with the changes observed when the modified buforin 2 interacts with cells.

The structural properties and dynamic behavior of the antimicrobial peptide melittin in hydrophobic and polar environments have been investigated. The main characteristics of the secondary structure of melittin in different media have been analyzed and compared with the data on an ideal α-helix. It has been shown that melittin is an α-helix bent in the region of Pro14; the N-terminus of the peptide tends to unfold, while the C-terminal segment (residues 14–23) retains a helical structure for 20 ns of the simulation. 2,2,2-Trifluoroethanol molecules stabilize the helical structure of the peptide by lowering the dielectric constant of the environment and preferentially accumulating near particular sites of the polypeptide chain.

The structural properties and dynamic behavior of the antimicrobial peptide melittin in hydrophobic and polar environments have been investigated. The main characteristics of the secondary structure of melittin in different media have been analyzed, and compared with the data on the ideal alpha-helix. It has been shown that melittin is an alpha-helix bent in the region of residue Pro14; in this case, the N-terminus of the peptide tends to unfold, while the C-terminal segment (residues 14-23) retains the helical structure for 20 ns of the simulation. 2,2,2-Trifluoroethanol molecules stabilize the helical structure of the peptide through lowering the dielectric constant of the environment and preferential accumulation nearby particular segments of the polypeptide chain.