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      Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.

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          Abstract

          Melittin is a venom peptide that disrupts lipid bilayers at temperatures below the liquid-crystalline to gel phase transition temperature (Tc). Notably, the ability of melittin to disrupt acidic dimyristoylphosphatidylglycerol (DMPG) bilayers was weaker than its ability to disrupt neutral dimyristoylphosphatidylcholine bilayers. The structure and orientation of melittin bound to DMPG bilayers were revealed by analyzing the 13C chemical shift anisotropy of [1-13C]-labeled melittin obtained from solid-state 13C NMR spectra. 13C chemical shift anisotropy showed oscillatory shifts with the index number of residues. Analysis of the chemical shift oscillation properties indicated that melittin bound to a DMPG membrane adopts a bent α-helical structure with tilt angles for the N- and C-terminal helices of -32 and +30°, respectively. The transmembrane melittin in DMPG bilayers indicates that the peptide protrudes toward the C-terminal direction from the core region of the lipid bilayer to show a pseudotransmembrane bent α-helix. Molecular dynamics simulation was performed to characterize the structure and interaction of melittin with lipid molecules in DMPG bilayers. The simulation results indicate that basic amino acid residues in melittin interact strongly with lipid head groups to generate a pseudo-transmembrane alignment. The N-terminus is located within the lipid core region and disturbs the lower surface of the lipid bilayer.

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          Author and article information

          Journal
          J Phys Chem B
          The journal of physical chemistry. B
          American Chemical Society (ACS)
          1520-5207
          1520-5207
          March 02 2017
          : 121
          : 8
          Affiliations
          [1 ] Graduate School of Engineering, Yokohama National University , 79-5 Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan.
          [2 ] School of Engineering and Applied Sciences, National University of Mongolia , Ulaanbaatar 14201, Mongolia.
          [3 ] Department of Life Science, University of Hyogo , Harima Science Garden City, Kamigori, Hyogo 678-1297, Japan.
          Article
          10.1021/acs.jpcb.6b11207
          28165239
          4b82ddda-18e4-4c8b-827f-f372e2497d03
          History

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