Multiscale Simulations of the Antimicrobial Peptide Maculatin 1.1: Water Permeation through Disordered Aggregates

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• 作者：Daniel L. Parton ; Elena V. Akhmatskaya ; Mark S. P. Sansom
• 刊名：The Journal of Physical Chemistry B
• 出版年：2012
• 出版时间：July 26, 2012
• 年：2012
• 卷：116
• 期：29
• 页码：8485-8493
• 全文大小：506K
• 年卷期：v.116,no.29(July 26, 2012)
• ISSN：1520-5207

文摘

The antimicrobial peptide maculatin 1.1 (M1.1) is an amphipathic 伪-helix that permeabilizes lipid bilayers. In coarse-grained molecular dynamics (CG MD) simulations, M1.1 has previously been shown to form membrane-spanning aggregates in DPPC bilayers. In this study, a simple multiscale methodology has been applied to allow sampling of important regions of the free energy surface at higher resolution. Thus, by back-converting the CG configurations to atomistic representations, it is shown that water is able to permeate through the M1.1 aggregates. Investigation of aggregate stoichiometry shows that at least six peptides are required for water permeation. The aggregates are dynamically disordered structures, and water flux occurs through irregular, fluctuating channels. The results are discussed in relation to experimental data and other simulations of antimicrobial peptides.