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Nanoelectrospray based synthesis of large, transportable membranes with integrated membrane proteins.

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Title: Nanoelectrospray based synthesis of large, transportable membranes with integrated membrane proteins.
Authors: Wilm, Matthias1,2,3,4 (AUTHOR) matthias.wilm@ucd.ie
Source: Scientific Reports. 10/24/2024, Vol. 14 Issue 1, p1-13. 13p.
Subject Terms: *BILAYER lipid membranes, *MEMBRANE proteins, *BIOLOGICAL membranes, *LIQUID surfaces, *BUFFER solutions
Abstract: Membrane proteins tend to be difficult to study since they need to be integrated into a lipid bilayer membrane to function properly. This study presents a method to synthesize a macroscopically large and freely transportable membrane with integrated membrane proteins which is useful for studying membrane proteins and protein complexes in isolation. The method could serve as a blueprint for the production of larger quantities of functionalised membranes for integration into technical devices similar to the MinION DNA sequencer. It is possible to self-assemble larger biological membranes on solid surfaces. However, they cannot be removed from their solid support without destroying them. In transportable form, self-assembled membranes are limited to sizes of about 17 nm in nanodiscs. Here we electrospray a series of molecular layers onto the liquid surface of a buffer solution which creates a flat, liquid environment on the surface that directs the self-assembly of the membrane. This method enables us to experimentally control the membrane composition and to succeed in producing large membranes with integrated OmpG, a transmembrane pore protein. The technique is compatible with the assembly of membrane based protein complexes. Listeriolysin O and pneumolysin efficiently assemble into non-covalent membrane pore complexes of approximately 30 units or more within the surface layer. [ABSTRACT FROM AUTHOR]
Copyright of Scientific Reports is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Nanoelectrospray based synthesis of large, transportable membranes with integrated membrane proteins.
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  Data: <searchLink fieldCode="JN" term="%22Scientific+Reports%22">Scientific Reports</searchLink>. 10/24/2024, Vol. 14 Issue 1, p1-13. 13p.
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  Data: *<searchLink fieldCode="DE" term="%22BILAYER+lipid+membranes%22">BILAYER lipid membranes</searchLink><br />*<searchLink fieldCode="DE" term="%22MEMBRANE+proteins%22">MEMBRANE proteins</searchLink><br />*<searchLink fieldCode="DE" term="%22BIOLOGICAL+membranes%22">BIOLOGICAL membranes</searchLink><br />*<searchLink fieldCode="DE" term="%22LIQUID+surfaces%22">LIQUID surfaces</searchLink><br />*<searchLink fieldCode="DE" term="%22BUFFER+solutions%22">BUFFER solutions</searchLink>
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  Data: Membrane proteins tend to be difficult to study since they need to be integrated into a lipid bilayer membrane to function properly. This study presents a method to synthesize a macroscopically large and freely transportable membrane with integrated membrane proteins which is useful for studying membrane proteins and protein complexes in isolation. The method could serve as a blueprint for the production of larger quantities of functionalised membranes for integration into technical devices similar to the MinION DNA sequencer. It is possible to self-assemble larger biological membranes on solid surfaces. However, they cannot be removed from their solid support without destroying them. In transportable form, self-assembled membranes are limited to sizes of about 17 nm in nanodiscs. Here we electrospray a series of molecular layers onto the liquid surface of a buffer solution which creates a flat, liquid environment on the surface that directs the self-assembly of the membrane. This method enables us to experimentally control the membrane composition and to succeed in producing large membranes with integrated OmpG, a transmembrane pore protein. The technique is compatible with the assembly of membrane based protein complexes. Listeriolysin O and pneumolysin efficiently assemble into non-covalent membrane pore complexes of approximately 30 units or more within the surface layer. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Scientific Reports is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1038/s41598-024-76797-w
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      – Code: eng
        Text: English
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        PageCount: 13
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      – SubjectFull: BILAYER lipid membranes
        Type: general
      – SubjectFull: MEMBRANE proteins
        Type: general
      – SubjectFull: BIOLOGICAL membranes
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      – SubjectFull: LIQUID surfaces
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              Text: 10/24/2024
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