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      Ultrasensitive label-free detection of protein-membrane interaction exemplified by toxin-liposome insertion

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      Embargo Lift Date: 2023-04-04
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      Author(s)
      Schönfeldová, Tereza
      Okur, Halil İbrahim
      Dal Peraro, Matteo
      Maček, Peter
      Zuber, Benoît
      Roke, Sylvie
      Vezočnik, Valerija
      Iacovache, Ioan
      Cao, Chan
      Date
      2022-04-04
      Source Title
      Journal of Physical Chemistry Letters
      Electronic ISSN
      1948-7185
      Publisher
      American Chemical Society
      Volume
      13
      Issue
      14
      Pages
      3197 - 3201
      Language
      English
      Type
      Article
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      Abstract
      Measuring the high-affinity binding of proteins to liposome membranes remains a challenge. Here, we show an ultrasensitive and direct detection of protein binding to liposome membranes using high throughput second harmonic scattering (SHS). Perfringolysin O (PFO), a pore-forming toxin, with a highly membrane selective insertion into cholesterol-rich membranes is used. PFO inserts only into liposomes with a cholesterol concentration >30%. Twenty mole-percent cholesterol results in neither SHS-signal deviation nor pore formation as seen by cryo-electron microscopy of PFO and liposomes. PFO inserts into cholesterol-rich membranes of large unilamellar vesicles in an aqueous solution with Kd= (1.5 ± 0.2) × 10-12M. Our results demonstrate a promising approach to probe protein-membrane interactions below sub-picomolar concentrations in a label-free and noninvasive manner on 3D systems. More importantly, the volume of protein sample is ultrasmall (<10 μL). These findings enable the detection of low-abundance proteins and their interaction with membranes. © 2022 American Chemical Society. All rights reserved
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      http://hdl.handle.net/11693/111819
      Published Version (Please cite this version)
      https://dx.doi.org/10.1021/acs.jpclett.1c04011
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