Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide

Using total internal fluorescence microscopy, highly parallel measurements of single lipid vesicles unexpectedly reveal that a small fraction of vesicles rupture in multiple discrete steps when destabilized by a membrane-active peptide which is in contrast to classical solubilization models. To acco...

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Main Authors: Tabaei, Seyed Ruhollah, Cho, Nam-Joon
Other Authors: School of Materials Science & Engineering
Format: Article
Language:English
Published: 2016
Subjects:
Online Access:https://hdl.handle.net/10356/80927
http://hdl.handle.net/10220/40633
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-809272020-06-01T10:13:50Z Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide Tabaei, Seyed Ruhollah Cho, Nam-Joon School of Materials Science & Engineering School of Chemical and Biomedical Engineering Centre for Biomimetic Sensor Science Nanostructures Using total internal fluorescence microscopy, highly parallel measurements of single lipid vesicles unexpectedly reveal that a small fraction of vesicles rupture in multiple discrete steps when destabilized by a membrane-active peptide which is in contrast to classical solubilization models. To account for this surprizing kinetic behaviour, we identified that this vesicle subpopulation consists of multilamellar vesicles, and that the outermost lamella is more susceptible to rupture than unilamellar vesicles of even smaller size. This finding sheds light on the multiple ways in which membrane configuration can influence strain in the bilayer leaflet and contribute to nm-scale membrane curvature sensing. NRF (Natl Research Foundation, S’pore) NMRC (Natl Medical Research Council, S’pore) 2016-06-08T03:28:20Z 2019-12-06T14:17:34Z 2016-06-08T03:28:20Z 2019-12-06T14:17:34Z 2015 Journal Article Tabaei, S. R., & Cho, N. -J. (2015). Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide. Chemical Communications, 51, 10272-10275. 1359-7345 https://hdl.handle.net/10356/80927 http://hdl.handle.net/10220/40633 10.1039/C5CC02769A en Chemical Communications © 2015 The Royal Society of Chemistry.
institution Nanyang Technological University
building NTU Library
country Singapore
collection DR-NTU
language English
topic Nanostructures
spellingShingle Nanostructures
Tabaei, Seyed Ruhollah
Cho, Nam-Joon
Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide
description Using total internal fluorescence microscopy, highly parallel measurements of single lipid vesicles unexpectedly reveal that a small fraction of vesicles rupture in multiple discrete steps when destabilized by a membrane-active peptide which is in contrast to classical solubilization models. To account for this surprizing kinetic behaviour, we identified that this vesicle subpopulation consists of multilamellar vesicles, and that the outermost lamella is more susceptible to rupture than unilamellar vesicles of even smaller size. This finding sheds light on the multiple ways in which membrane configuration can influence strain in the bilayer leaflet and contribute to nm-scale membrane curvature sensing.
author2 School of Materials Science & Engineering
author_facet School of Materials Science & Engineering
Tabaei, Seyed Ruhollah
Cho, Nam-Joon
format Article
author Tabaei, Seyed Ruhollah
Cho, Nam-Joon
author_sort Tabaei, Seyed Ruhollah
title Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide
title_short Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide
title_full Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide
title_fullStr Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide
title_full_unstemmed Lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide
title_sort lamellar sheet exfoliation of single lipid vesicles by a membrane-active peptide
publishDate 2016
url https://hdl.handle.net/10356/80927
http://hdl.handle.net/10220/40633
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