ISSN:
1432-2234
Keywords:
Key words: Model peptides
;
Monolayers
;
Penetration depth
;
Modelling
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract. Molecular modelling calculations based on experimental data obtained in solution and in small unilamellar vesicles are used to study interactions between amphiphilic basic peptides and membranes. The behaviour of such peptides during the initial and final stages of the adsorption process is our primary interest. Primary sequences of 20 amino acid residues were designed with equal numbers of basic lysines and hydrophobic leucines in order to get an amphipathic α helix. First, in solution, aggregates with an increasing number (up to nine) of helical monomers were built up and the hydrophobic solvent accessible surface per monomer was analysed on energy minimised structures. This showed that aggregates with 5–8 of monomers should be equally probable, in reasonable accordance with experimental data. In addition, models of membranes with 21 dimyristoyl-phosphatidylcholine lipids were constructed; amphiphilic peptides were merged into these assemblies with their axes parallel to the monolayer surface and the whole lipid/peptide complex was submitted to a few steps of simulated annealing and further energy minimisation techniques in order to equilibrate alkyl chains in the vicinity of the peptide. These simulations yield an estimation of the penetration depth for the peptide in the monolayer of ∼3.2 Å, whereas experimental approaches to this question were not productive. The modification in the peptide net electrical charge by interchanging Leu in Lys residues in such systems is also examined: for low-charged peptides the penetration depth increases.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002140050413
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