A Molecular Dynamics Study of Antimicrobial Peptide Interactions with the Lipopolysaccharides of the Outer Bacterial Membrane

[1] Abraham MJ(2015)GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers SoftwareX 1 19-25

[2] Murtola T(2009)Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics Biochemistry 48 8083-8093

[3] Schulz R(2016)Antimicrobial peptide potency is facilitated by greater conformational flexibility when binding to gram-negative bacterial inner membranes Sci Rep 6 1-13

[4] Páll S(1992)Shortened cecropin a-melittin hybrids significant size reduction retains potent antibiotic activity FEBS Lett 296 190-194

[5] Smith JC(2021)In vitro and in vivo toxicity and antibacterial efficacy of melittin against clinical extensively drug-resistant bacteria BMC Pharmacol Toxicol 22 1-12

[6] Hess B(2016)Antimicrobial peptide simulations and the influence of force field on the free energy for pore formation in lipid bilayers J Chem Theory Comput 12 4524-4533

[7] Lindahl E(1998)Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane Biophys J 75 1603-1618

[8] Almeida PF(2005)Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3 238-250

[9] Pokorny A(2016)The free energy of small solute permeation through the Escherichia coli outer membrane has a distinctly asymmetric profile J Phys Chem Lett 7 3446-3451

[10] Amos S-BT(2020)Molecular dynamics simulation of the interaction of two linear battacin analogs with model gram-positive and gram-negative bacterial cell membranes ACS Omega 6 388-400

[1] Abraham MJ(2015)GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers SoftwareX 1 19-25

[2] Murtola T(2009)Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics Biochemistry 48 8083-8093

[3] Schulz R(2016)Antimicrobial peptide potency is facilitated by greater conformational flexibility when binding to gram-negative bacterial inner membranes Sci Rep 6 1-13

[4] Páll S(1992)Shortened cecropin a-melittin hybrids significant size reduction retains potent antibiotic activity FEBS Lett 296 190-194

[5] Smith JC(2021)In vitro and in vivo toxicity and antibacterial efficacy of melittin against clinical extensively drug-resistant bacteria BMC Pharmacol Toxicol 22 1-12

[6] Hess B(2016)Antimicrobial peptide simulations and the influence of force field on the free energy for pore formation in lipid bilayers J Chem Theory Comput 12 4524-4533

[7] Lindahl E(1998)Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane Biophys J 75 1603-1618

[8] Almeida PF(2005)Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3 238-250

[9] Pokorny A(2016)The free energy of small solute permeation through the Escherichia coli outer membrane has a distinctly asymmetric profile J Phys Chem Lett 7 3446-3451

[10] Amos S-BT(2020)Molecular dynamics simulation of the interaction of two linear battacin analogs with model gram-positive and gram-negative bacterial cell membranes ACS Omega 6 388-400