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Single Vesicle Analysis Reveals Nanoscale Membrane Curvature Selective Pore Formation in Lipid Membranes by an Antiviral α-Helical Peptide

Seyed Tabaei (Institutionen för teknisk fysik, Biologisk fysik) ; Michael Rabe (Institutionen för teknisk fysik, Biologisk fysik) ; Vladimir P. Zhdanov (Kompetenscentrum katalys (KCK)) ; Nam-Joon Cho ; Fredrik Höök (Institutionen för teknisk fysik, Biologisk fysik)
Nano letters (1530-6984). Vol. 12 (2012), 11, p. 5719–5725.
[Artikel, refereegranskad vetenskaplig]

Using tethered sub-100 nm lipid vesicles that mimic enveloped viruses with nanoscale membrane curvature, we have in this work designed a total internal reflection fluorescence microscopy-based single vesicle assay to investigate how an antiviral amphipathic α-helical (AH) peptide interacts with lipid membranes to induce membrane curvature-dependent pore formation and membrane destabilization. Based on a combination of statistics from single vesicle imaging, binding kinetics data, and theoretical analysis, we propose a mechanistic model that is consistent with the experimentally observed peptide association and pore formation kinetics at medically relevant peptide concentrations (10 nM to 1 μM) and unusually low peptide-to-lipid (P/L) ratio (∼1/1000). Importantly, the preference of the AH peptide to selectively rupture virions with sub-100 nm diameters appears to be related to membrane strain-dependent pore formation rather than to previously observed nanoscale membrane curvature facilitated binding of AH peptides. Compared to other known proteins and peptides, the combination of low effective P/L ratio and high specificity for nm-sized membrane curvature lends this particular AH peptide great potential to serve as a framework for developing a highly specific and potent antiviral agent for prophylactic and therapeutic applications while avoiding toxic side effects against host cell membranes.

Nyckelord: Single molecule fluorescence microscopy, lipid vesicles, peptide nucleation, pore formation, membrane curvature, antiviral peptides

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Denna post skapades 2012-11-22. Senast ändrad 2013-01-18.
CPL Pubid: 166482


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Institutioner (Chalmers)

Institutionen för teknisk fysik, Biologisk fysik (2007-2015)
Kompetenscentrum katalys (KCK)


Nanovetenskap och nanoteknik
Biologiska vetenskaper

Chalmers infrastruktur

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