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Title of Journal: Eur Biophys J

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Abbravation: European Biophysics Journal

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Springer-Verlag

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10.1007/pl00002871

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1432-1017

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A molecular dynamics study of the bee venom melitt

Authors: Alice Glättli Indira Chandrasekhar Wilfred F van Gunsteren
Publish Date: 2005/12/02
Volume: 35, Issue: 3, Pages: 255-267
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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 3Jcoupling constants Generally it appears that higher the stability of the helical conformation of melittin lower is the dielectric permittivity of the environment In addition peptidelipid interactions were investigated showing that the Cterminus of the peptide provides an anchor to the lipid bilayer by forming hydrogen bonds with the lipid head groupsFinancial support was obtained through the National Center of Competence in Research NCCR Structural Biology of the Swiss National Science Foundation which is gratefully acknowledged AG thanks Dr Bojan Zagrovic and Dr Chris Oostenbrink for fruitful discussions


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