期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 116, 期 29, 页码 8485-8493出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp212358y
关键词
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资金
- BBSRC
- Fujitsu Laboratories of Europe
- Wellcome Trust
- BBSRC [BB/I019855/1, BB/H000267/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BEP17032, BB/H000267/1, BBS/B/16011, B19456, BB/I019855/1] Funding Source: researchfish
The antimicrobial peptide maculatin 1.1 (M1.1) is an amphipathic alpha-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.
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