ArticleEuropean biophysics journal : EBJ2006
A molecular dynamics study of the bee venom melittin in aqueous solution, in methanol, and inserted in a phospholipid bilayer.
Article in European biophysics journal : EBJ, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 45 citations in OpenAlex.
- Liposome Deformation Induced by Membrane-Binding Peptides.Micromachines · 2023Article
- A new therapeutic approach for bone metastasis in colorectal cancer: intratumoral melittin.The journal of venomous animals and toxins including tropical diseases · 2022Article
- Hyaluronic Acid Coating Reduces the Leakage of Melittin Encapsulated in Liposomes and Increases Targeted Delivery to Melanoma Cells.Pharmaceutics · 2021Article
- Constitutive expression of a novel antimicrobial protein, Hcm1, confers resistance to both Verticillium and Fusarium wilts in cotton.Scientific reports · 2016Article
- Measuring melittin uptake into hydrogel nanoparticles with near-infrared single nanoparticle surface plasmon resonance microscopy.Analytical chemistry · 2015Article
- Article
- A novel antimicrobial protein for plant protection consisting of a Xanthomonas oryzae harpin and active domains of cecropin A and melittin.Microbial biotechnology · 2011Article
- Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.The journal of physical chemistry. B · 2011Article
- Conformational sampling of peptides in cellular environments.Biophysical journal · 2008Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural properties of melittin, a small amphipathic peptide found in the bee venom, are investigated in three different environments by molecular dynamics simulation. Long simulations have been performed for monomeric melittin solvated in water, in methanol, and shorter ones for melittin inserted in a dimyristoylphosphatidylcholine bilayer. The resulting trajectories were analysed in terms of structural properties of the peptide and compared to the available NMR data. While in water and methanol solution melittin is observed to partly unfold, the peptide retains its structure when embedded in a lipid bilayer. The latter simulation shows good agreement with the experimentally derived (3)J-coupling constants. Generally, it appears that higher the stability of the helical conformation of melittin, lower is the dielectric permittivity of the environment. In addition, peptide-lipid interactions were investigated showing that the C-terminus of the peptide provides an anchor to the lipid bilayer by forming hydrogen bonds with the lipid head groups.
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