dc.contributor.authorTabaei, Seyed R.
dc.contributor.authorRabe, Michael
dc.contributor.authorZhdanov, Vladimir P.
dc.contributor.authorCho, Nam-Joon
dc.contributor.authorHöök, Fredrik
dc.date.accessioned2013-07-10T03:21:21Z
dc.date.available2013-07-10T03:21:21Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationTabaei, S. R., Rabe, M., Zhdanov, V. P., Cho, N.-J., Höök, F. (2012). Single vesicle analysis reveals nanoscale membrane curvature selective pore formation in lipid membranes by an antiviral α-helical peptide. Nano Letters, 12(11), 5719-5725.
dc.identifier.urihttp://hdl.handle.net/10220/11090
dc.description.abstractUsing 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.en_US
dc.description.sponsorshipNMRC (Natl Medical Research Council, S’pore)
dc.language.isoenen_US
dc.relation.ispartofseriesNano lettersen_US
dc.rights© 2012 American Chemical Society.en_US
dc.titleSingle vesicle analysis reveals nanoscale membrane curvature selective pore formation in lipid membranes by an antiviral α-helical peptideen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Materials Science and Engineeringen_US
dc.identifier.doihttp://dx.doi.org/10.1021/nl3029637


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