ArticleBiophysical journal2008
Coarse-grained simulations of the membrane-active antimicrobial Peptide maculatin 1.1.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Unlocking the power of membrane biophysics: enhancing the study of antimicrobial peptides activity and selectivity.Biophysical reviews · 2025Review
- Membrane-Active Antibiotics Affect Domains in Bacterial Membranes as the First Step of Their Activity.Nano letters · 2024Article
- Vesicle protrusion induced by antimicrobial peptides suggests common carpet mechanism for short antimicrobial peptides.Scientific reports · 2024Article
- Organizations of melittin peptides after spontaneous penetration into cell membranes.Biophysical journal · 2022Article
- Antimicrobial Peptides: An Update on Classifications and Databases.International journal of molecular sciences · 2021Review
- Article
- The Location of the Antimicrobial Peptide Maculatin 1.1 in Model Bacterial Membranes.Frontiers in chemistry · 2020Article
- A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures.Journal of molecular modeling · 2018Article
- Differential Interaction of Antimicrobial Peptides with Lipid Structures Studied by Coarse-Grained Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2017Article
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.Biophysical journal · 2017Article
- Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Frontiers in neuroscience · 2017Review
- Coarse-grained simulations of hemolytic peptide δ-lysin interacting with a POPC bilayer.Biochimica et biophysica acta · 2016Article
- Lipid molecules can induce an opening of membrane-facing tunnels in cytochrome P450 1A2.Physical chemistry chemical physics : PCCP · 2016Article
- Article
- Article
- Interaction of the antimicrobial peptide polymyxin B1 with both membranes of E. coli: a molecular dynamics study.PLoS computational biology · 2015Article
- LipidWrapper: an algorithm for generating large-scale membrane models of arbitrary geometry.PLoS computational biology · 2014Article
- Peptide-lipid interactions: experiments and applications.International journal of molecular sciences · 2013Article
- Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Cellular and molecular life sciences : CMLS · 2011Review
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4 authors.
Funding
Abstract
Maculatin 1.1 (M1.1) is a membrane-active antimicrobial peptide (AMP) from an Australian tree frog that forms a kinked amphipathic alpha-helix in the presence of a lipid bilayer or bilayer-mimetic environment. To help elucidate its mechanism of membrane-lytic activity, we performed a total of approximately 8 micros of coarse-grained molecular dynamics (CG-MD) simulations of M1.1 in the presence of zwitterionic phospholipid membranes. Several systems were simulated in which the peptide/lipid ratio was varied. At a low peptide/lipid ratio, M1.1 adopted a kinked, membrane-interfacial location, consistent with experiment. At higher peptide/lipid ratios, we observed spontaneous, cooperative membrane insertion of M1.1 peptide aggregates. The minimum size for formation of a transmembrane (TM) aggregate was just four peptides. The absence of a simple and well-defined central channel, along with the exclusion of lipid headgroups from the aggregates, suggests that a pore-like model is an unlikely explanation for the mechanism of membrane lysis by M1.1. We also performed an extended 1.25 micros simulation of the permeabilization of a complete liposome by multiple peptides. Consistent with the simpler bilayer simulations, formation of monomeric interfacial peptides and TM peptide clusters was observed. In contrast, major structural changes were observed in the vesicle membrane, implicating induced membrane curvature in the mechanism of active antimicrobial peptide lysis. This contrasted with the behavior of the nonpore-forming model peptide WALP23, which inserted into the vesicle to form extended clusters of TM alpha-helices with relatively little perturbation of bilayer properties.
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