Aggregation of oligoarginines at phospholipid membranes: Molecular dynamics simulations, time-dependent fluorescence shift, and biomimetic colorimetric assays

Mario Vazdar, Erik Wernersson, Morteza Khabiri, Lukasz Cwiklik, Piotr Jurkiewicz, Martin Hof, Ella Mann, Sofiya Kolusheva, Raz Jelinek, Pavel Jungwirth

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)11530-11540
Number of pages11
JournalJournal of Physical Chemistry B
Volume117
Issue number39
DOIs
StatePublished - 3 Oct 2013

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