title: Electrostatics and flexibility drive membrane recognition and early penetration by the antimicrobial peptide dendrimer bH1.
abstract: Molecular dynamics simulations of the polycationic antimicrobial peptide dendrimer (Leu)8(DapLeu)4(DapPhe)2DapLys-NH2 binding to membranes suggest that electrostatic interactions with the polyanionic lipopolysaccharide (LPS) and conformational flexibility of the 2,3-diaminopropanoic acid (Dap) branching units drive its selective insertion into microbial membranes.
authors: Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. michele.cascella@iac.unibe.ch.
authors: Harish K
authors: HK
authors: Ravi
authors: Michaela
authors: M
authors: Stach
authors: Thereza A
authors: TA
authors: Soares
authors: Tamis
authors: T
authors: Darbre
authors: Jean-Louis
authors: JL
authors: Reymond
authors: Michele
authors: M
authors: Cascella
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects / Q000378:metabolism*; D050091:Dendrimers / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D008070:Lipopolysaccharides / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D055672:Static Electricity; D015091:beta-Alanine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D050091:Dendrimers; D008070:Lipopolysaccharides; D015091:beta-Alanine; C011757:2,3-diaminopropionic acid