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The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action
- Source :
- European Biophysics Journal
- Publication Year :
- 2011
- Publisher :
- Springer Science and Business Media LLC, 2011.
-
Abstract
- Short cationic antimicrobial peptides (AMPs) are believed to act either by inducing transmembrane pores or disrupting membranes in a detergent-like manner. For example, the antimicrobial peptides aurein 1.2, citropin 1.1, maculatin 1.1 and caerin 1.1, despite being closely related, appear to act by fundamentally different mechanisms depending on their length. Using molecular dynamics simulations, the structural properties of these four peptides have been examined in solution as well as in a variety of membrane environments. It is shown that each of the peptides has a strong preference for binding to regions of high membrane curvature and that the structure of the peptides is dependent on the degree of local curvature. This suggests that the shorter peptides aurein 1.2 and citropin 1.1 act via a detergent-like mechanism because they can induce high local, but not long-range curvature, whereas the longer peptides maculatin 1.1 and caerin 1.1 require longer range curvature to fold and thus bind to and stabilize transmembrane pores.
- Subjects :
- Protein Conformation
Stereochemistry
Lipid Bilayers
Antimicrobial peptides
Biophysics
Membrane biology
Molecular Dynamics Simulation
Biology
Amphibian Proteins
Lipid bilayer
Cell membrane
GROMOS
Anti-Infective Agents
Secondary structure
medicine
Original Paper
Antiinfective agent
Binding Sites
Curvature
Circular Dichroism
Cell Membrane
General Medicine
Transmembrane protein
Membrane
medicine.anatomical_structure
Membrane curvature
Antimicrobial Cationic Peptides
Subjects
Details
- ISSN :
- 14321017 and 01757571
- Volume :
- 40
- Database :
- OpenAIRE
- Journal :
- European Biophysics Journal
- Accession number :
- edsair.doi.dedup.....d418ac97e3acd639030be67e4b71b8d5