Electrostatics and flexibility drive membrane recognition and early penetration by the antimicrobial peptide dendrimer bH1

Chem Commun (Camb). 2013 Oct 9;49(78):8821-3. doi: 10.1039/c3cc44912b.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / metabolism*
  • Anti-Infective Agents / pharmacology
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / metabolism*
  • Antimicrobial Cationic Peptides / pharmacology
  • Bacteria / drug effects
  • Bacteria / metabolism*
  • Dendrimers / chemistry
  • Dendrimers / metabolism*
  • Dendrimers / pharmacology
  • Lipopolysaccharides / metabolism*
  • Molecular Dynamics Simulation
  • Static Electricity
  • beta-Alanine / analogs & derivatives
  • beta-Alanine / chemistry
  • beta-Alanine / metabolism
  • beta-Alanine / pharmacology

Substances

  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Dendrimers
  • Lipopolysaccharides
  • beta-Alanine
  • 2,3-diaminopropionic acid