Improvement of outer membrane-permeabilizing and lipopolysaccharide-binding activities of an antimicrobial cationic peptide by C-terminal modification.

Lignende værker

• NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION
  af: Bhunia, Anirban, et al.
  Udgivet: (2010)
• Bordetella pertussis Lipid A Glucosamine Modification Confers Resistance to Cationic Antimicrobial Peptides and Increases Resistance to Outer Membrane Perturbation
  af: Shah, Nita R., et al.
  Udgivet: (2014)
• A Lack of Synergy Between Membrane-permeabilizing Cationic Antimicrobial Peptides and Conventional Antibiotics
  af: He, Jing, et al.
  Udgivet: (2014)
• Antimicrobial Peptides: Insights into Membrane Permeabilization, Lipopolysaccharide Fragmentation and Application in Plant Disease Control
  af: Datta, Aritreyee, et al.
  Udgivet: (2015)
• The Role of Outer Membrane Proteins and Lipopolysaccharides for the Sensitivity of Escherichia coli to Antimicrobial Peptides
  af: Ebbensgaard, Anna, et al.
  Udgivet: (2018)