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

Authors
  • Ravi, Harish K
  • Stach, Michaela
  • Soares, Thereza A
  • Darbre, Tamis
  • Reymond, Jean-Louis
  • Cascella, Michele
Type
Published Article
Journal
Chemical Communications
Publisher
The Royal Society of Chemistry
Publication Date
Oct 09, 2013
Volume
49
Issue
78
Pages
8821–8823
Identifiers
DOI: 10.1039/c3cc44912b
PMID: 23959139
Source
Medline
License
Unknown

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.

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