riDOM, a cell penetrating peptide : interaction with phospholipid bilayers

Québatte, Gabriela and Kitas, Eric and Seelig, Joachim. (2013) riDOM, a cell penetrating peptide : interaction with phospholipid bilayers. BBA - Biochimica et Biophysica Acta, 1838 (3). pp. 968-977.

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Official URL: http://edoc.unibas.ch/dok/A6211866

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Melittin is an amphipathic peptide which has received much attention as a model peptide for peptide-membrane interactions. It is however not suited as a transfection agent due to its cytolytic and toxicological effects. Retro-inverso-melittin, when covalently linked to the lipid 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (riDOM), eliminates these shortcomings. The interaction of riDOM with phospholipid membranes was investigated with circular dichroism (CD) spectroscopy, dynamic light scattering, ζ-potential measurements, and high-sensitivity isothermal titration calorimetry. riDOM forms cationic nanoparticles with a diameter of ~13nm which are well soluble in water and bind with high affinity to DNA and lipid membranes. When dissolved in bilayer membranes, riDOM nanoparticles dissociate and form transient pores. riDOM-induced membrane leakiness is however much reduced compared to that of authentic melittin. The secondary structure of the ri-melittin is not changed when riDOM is transferred from water to the membrane and displays a large fraction of β-structure. The (31)P NMR spectrum of the nanoparticle is however transformed into a typical bilayer spectrum. The Gibbs free energy of riDOM binding to bilayer membranes is -8.0 to -10.0kcal/mol which corresponds to the partition energy of just one fatty acyl chain. Half of the hydrophobic surface of the riDOM lipid extension with its 2 oleic acyl chains is therefore involved in a lipid-peptide interaction. This packing arrangement guarantees a good solubility of riDOM both in the aqueous and in the membrane phase. The membrane binding enthalpy is small and riDOM binding is thus entropy-driven.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum
UniBasel Contributors:Québatte, Gabriela and Seelig, Joachim
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:14 Nov 2017 09:39
Deposited On:31 Jan 2014 09:51

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