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• W2765995714 abstract "Membrane-active peptides (MAPs) are able to induce pores in cell membranes via molecular mechanisms, which are still subject to ongoing research. In this work, we present molecular dynamics simulations that suggest a precursor membrane defect plays an important role in the pore-inducing activity of the prototypical antimicrobial peptide melittin. The simulations reveal that the hydrophobic N-terminus of melittin is able to recognize and insert into the membrane defect in the lipid bilayer and that this leads to a cascading transfer of adsorbed peptides to the membrane defect, leading to peptide aggregation in the pore. We show that this mechanism also acts in the case of a melittin mutant without the flexible central proline hinge, thus indicating the latter is not crucial to the activity of melittin, which is consistent with experiments." @default.
• W2765995714 created "2017-11-10" @default.
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• W2765995714 date "2017-10-31" @default.
• W2765995714 modified "2023-09-29" @default.
• W2765995714 title "Molecular Simulations of Melittin-Induced Membrane Pores" @default.
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• W2765995714 doi "https://doi.org/10.1021/acs.jpcb.7b07126" @default.
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