Aggregation of Oligoarginines at Phospholipid Membranes: Molecular Dynamics Simulations, Time-Dependent Fluorescence Shift, and Biomimetic Colorimetric Assays
| Autor: | Piotr Jurkiewicz, Lukasz Cwiklik, Mario Vazdar, Morteza Khabiri, Martin Hof, Sofiya Kolusheva, Erik Wernersson, Raz Jelinek, Ella Mann, Pavel Jungwirth |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Arginine
Polymers Lipid Bilayers Lysine Phospholipid Peptide Phosphatidylserines Molecular Dynamics Simulation Fluorescence Membrane Potentials Molecular dynamics chemistry.chemical_compound Biomimetics 2-Naphthylamine Materials Chemistry Physical and Theoretical Chemistry Phospholipids Fluorescent Dyes chemistry.chemical_classification Bilayer Polyynes Dextrans Mycophenolic Acid Polyacetylene Polymer Surfaces Coatings and Films Amino acid arginine cell penetrating peptides aggregation molecular dynamics simulations solvent relaxation biomimetic assays Membrane Biochemistry chemistry Phosphatidylcholines Biophysics Colorimetry Adsorption Peptides Laurates |
| Zdroj: | The Journal of Physical Chemistry B. 117:11530-11540 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/jp405451e |
| Popis: | A time-dependent fluorescence shift method, biomimetic colorimetric assays, and molecular dynamics simulations have been performed in search of explanations why arginine rich peptides with intermediate lengths of about 10 amino acids translocate well through cellular membranes, while analogous lysine rich peptides do not. First, we demonstrate that an important factor for efficient peptide adsorption, as the first prerequisite for translocation across the membrane, is the presence of negatively charged phospholipids in the bilayer. Second, we observe a strong tendency of adsorbed arginine (but not lysine) containing peptides to aggregate at the bilayer surface. We suggest that this aggregation of oligoarginines leads to partial disruption of the bilayer integrity due to the accumulated large positive charge at its surface, which increases membrane-surface interactions due to the increased effective charge of the aggregates. As a result, membrane penetration and translocation of medium length oligoarginines becomes facilitated in comparison to single arginine and very long polyarginines, as well as to lysine containing peptides. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|