Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces

•[K108W111]107–115 hLz has an increased affinity toward neutral and negative membranes.•[K108W111]107–115 hLz induces a reorganization of the membrane while interacts.•Together the electrostatic and hydrophobic interactions explain the enhanced activity. Substitution of Ala 108 and Ala 111 in the 10...

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Veröffentlicht in:	Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2014-02, Vol.114, p.363-371
Hauptverfasser:	Bouchet, Ana M., Iannucci, Nancy B., Pastrian, María B., Cascone, Osvaldo, Santos, Nuno C., Disalvo, Edgardo A., Hollmann, Axel
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anti-Bacterial Agents - pharmacology Antimicrobial peptide Fluorescence Humans Kinetics Lipid Bilayers - chemistry Lysozyme Membranes, Artificial Molecular Sequence Data Peptides - chemistry Peptides - pharmacology Peptide–membrane interactions, Hydrophilic–hydrophobic synergism Phospholipids - chemistry Pressure Sequence Alignment Static Electricity Tryptophan - metabolism
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