title: Theoretical insight into the relationship between the structures of antimicrobial peptides and their actions on bacterial membranes.
abstract: Antimicrobial peptides with diverse cationic charges, amphiphathicities, and secondary structures possess a variety of antimicrobial activities against bacteria, fungi, and other generalized targets. To illustrate the relationship between the structures of these peptide and their actions at microscopic level, we present systematic coarse-grained dissipative particle dynamics simulations of eight types of antimicrobial peptides with different secondary structures interacting with a lipid bilayer membrane. We find that the peptides use multiple mechanisms to exert their membrane-disruptive activities: A cationic charge is essential for the peptides to selectively target negatively charged bacterial membranes. This cationic charge is also responsible for promoting electroporation. A significant hydrophobic portion is necessary to disrupt the membrane through formation of a permeable pore or translocation. Alternatively, the secondary structure and the corresponding rigidity of the peptides determine the pore structure and the translocation pathway.
authors: Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, College of Chemistry, Beijing Normal University , Xin-wai-da-jie 19#, Beijing 100875, China.
authors: Licui
authors: L
authors: Chen
authors: Xiaoxu
authors: X
authors: Li
authors: Lianghui
authors: L
authors: Gao
authors: Weihai
authors: W
authors: Fang
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D001419:Bacteria / Q000166:cytology* / Q000187:drug effects; D002462:Cell Membrane / Q000187:drug effects* / Q000378:metabolism; D008051:Lipid Bilayers / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D016062:Porosity; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers