title: [Effect of Pro11-Ala11 amino acid substitution on structural and functional properties of antimicrobial peptide buforin 2].
abstract: 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.
authors.forename: T V
authors.initials: TV
authors.lastname: Naumenkova
authors.forename: M Iu
authors.initials: MIu
authors.lastname: Antonov
authors.forename: I N
authors.initials: IN
authors.lastname: Nikolaev
authors.forename: K V
authors.initials: KV
authors.lastname: Shaĭtan
mesh_terms: D000409:Alanine / Q000737:chemistry; D019943:Amino Acid Substitution; D000890:Anti-Infective Agents / Q000737:chemistry* / Q000378:metabolism; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism; D006860:Hydrogen Bonding; D011392:Proline / Q000737:chemistry; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D014867:Water / Q000737:chemistry
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; C097849:buforin II; D014867:Water; D011392:Proline; D000409:Alanine