The effect of membrane curvature on the conformation of antimicrobial peptides: Implications for binding and the mechanism of action

Chen, Rong and Mark, Alan E. (2011) The effect of membrane curvature on the conformation of antimicrobial peptides: Implications for binding and the mechanism of action. European Biophysics Journal, 40 4: 545-553. doi:10.1007/s00249-011-0677-4


Author Chen, Rong
Mark, Alan E.
Title The effect of membrane curvature on the conformation of antimicrobial peptides: Implications for binding and the mechanism of action
Journal name European Biophysics Journal   Check publisher's open access policy
ISSN 0175-7571
Publication date 2011-04-01
Sub-type Article (original research)
DOI 10.1007/s00249-011-0677-4
Volume 40
Issue 4
Start page 545
End page 553
Total pages 9
Place of publication Germany
Publisher Springer
Collection year 2012
Language eng
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.
Keyword Antimicrobial peptides
Curvature
GROMOS
Lipid bilayer
Molecular dynamics simulation
Secondary structure
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Mon, 03 Oct 2011, 20:39:35 EST by Professor Alan Mark on behalf of School of Chemistry & Molecular Biosciences