The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action |
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Authors: | Rong?Chen Email author" target="_blank">Alan?E?MarkEmail author |
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Institution: | (1) School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, 4072, Australia;(2) Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia; |
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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. |
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Keywords: | |
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