Electrostatics and flexibility drive membrane recognition and early penetration by the antimicrobial peptide dendrimer bH1.
- Ravi HK Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. michele.cascella@iac.unibe.ch.
- Stach M
- Soares TA
- Darbre T
- Reymond JL
- Cascella M
- 2013-08-21
Published in:
- Chemical communications (Cambridge, England). - 2013
Anti-Infective Agents
Antimicrobial Cationic Peptides
Bacteria
Dendrimers
Lipopolysaccharides
Molecular Dynamics Simulation
Static Electricity
beta-Alanine
English
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.
- Language
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- English
- Open access status
- green
- Identifiers
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- DOI 10.1039/c3cc44912b
- PMID 23959139
- Persistent URL
- https://sonar.ch/global/documents/218951
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