Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs

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Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs. / Johansen, Nicolai Tidemand; Luchini, Alessandra; Tidemand, Frederik Grønbæk; Orioli, Simone; Martel, Anne; Porcar, Lionel; Arleth, Lise; Pedersen, Martin Cramer.

In: Langmuir, Vol. 37, No. 22, 2021, p. 6681-6690.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Johansen, NT, Luchini, A, Tidemand, FG, Orioli, S, Martel, A, Porcar, L, Arleth, L & Pedersen, MC 2021, 'Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs', Langmuir, vol. 37, no. 22, pp. 6681-6690. https://doi.org/10.1021/acs.langmuir.1c00560

APA

Johansen, N. T., Luchini, A., Tidemand, F. G., Orioli, S., Martel, A., Porcar, L., Arleth, L., & Pedersen, M. C. (2021). Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs. Langmuir, 37(22), 6681-6690. https://doi.org/10.1021/acs.langmuir.1c00560

Vancouver

Johansen NT, Luchini A, Tidemand FG, Orioli S, Martel A, Porcar L et al. Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs. Langmuir. 2021;37(22):6681-6690. https://doi.org/10.1021/acs.langmuir.1c00560

Author

Johansen, Nicolai Tidemand ; Luchini, Alessandra ; Tidemand, Frederik Grønbæk ; Orioli, Simone ; Martel, Anne ; Porcar, Lionel ; Arleth, Lise ; Pedersen, Martin Cramer. / Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs. In: Langmuir. 2021 ; Vol. 37, No. 22. pp. 6681-6690.

Bibtex

@article{cb9a724e722b4a80bbcfa926d43402a8,
title = "Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs",
abstract = "Nanodiscs based on membrane scaffold proteins (MSPs) and phospholipids are used as membrane mimics to stabilize membrane proteins in solution for structural and functional studies. Combining small-angle X-ray scattering (SAXS), differential scanning calorimetry (DSC), and time-resolved small-angle neutron scattering (TR-SANS), we characterized the structure and lipid bilayer properties of five different nanodiscs made with dimyristoylphosphatidylcholine and different MSPs varying in size, charge, and circularization. Our SAXS modeling showed that the structural parameters of the embedded lipids are all similar, irrespective of the MSP properties. DSC showed that the lipid packing is not homogeneous in the nanodiscs and that a 20 {\AA} wide boundary layer of lipids with perturbed packing is located close to the MSP, while the packing of central lipids is tighter than in large unilamellar vesicles. Finally, TR-SANS showed that lipid exchange rates in nanodiscs decrease with increasing nanodisc size and are lower for the nanodiscs made with supercharged MSPs compared to conventional nanodiscs. Altogether, the results provide a thorough biophysical understanding of the nanodisc as a model membrane system, which is important in order to carry out and interpret experiments on membrane proteins embedded in such systems. ",
author = "Johansen, {Nicolai Tidemand} and Alessandra Luchini and Tidemand, {Frederik Gr{\o}nb{\ae}k} and Simone Orioli and Anne Martel and Lionel Porcar and Lise Arleth and Pedersen, {Martin Cramer}",
note = "Funding Information: The work was funded by the Lundbeck Foundation Brainstruc Programme (R155-2015-2666). Publisher Copyright: {\textcopyright} 2021 American Chemical Society.",
year = "2021",
doi = "10.1021/acs.langmuir.1c00560",
language = "English",
volume = "37",
pages = "6681--6690",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "22",

}

RIS

TY - JOUR

T1 - Structural and Biophysical Properties of Supercharged and Circularized Nanodiscs

AU - Johansen, Nicolai Tidemand

AU - Luchini, Alessandra

AU - Tidemand, Frederik Grønbæk

AU - Orioli, Simone

AU - Martel, Anne

AU - Porcar, Lionel

AU - Arleth, Lise

AU - Pedersen, Martin Cramer

N1 - Funding Information: The work was funded by the Lundbeck Foundation Brainstruc Programme (R155-2015-2666). Publisher Copyright: © 2021 American Chemical Society.

PY - 2021

Y1 - 2021

N2 - Nanodiscs based on membrane scaffold proteins (MSPs) and phospholipids are used as membrane mimics to stabilize membrane proteins in solution for structural and functional studies. Combining small-angle X-ray scattering (SAXS), differential scanning calorimetry (DSC), and time-resolved small-angle neutron scattering (TR-SANS), we characterized the structure and lipid bilayer properties of five different nanodiscs made with dimyristoylphosphatidylcholine and different MSPs varying in size, charge, and circularization. Our SAXS modeling showed that the structural parameters of the embedded lipids are all similar, irrespective of the MSP properties. DSC showed that the lipid packing is not homogeneous in the nanodiscs and that a 20 Å wide boundary layer of lipids with perturbed packing is located close to the MSP, while the packing of central lipids is tighter than in large unilamellar vesicles. Finally, TR-SANS showed that lipid exchange rates in nanodiscs decrease with increasing nanodisc size and are lower for the nanodiscs made with supercharged MSPs compared to conventional nanodiscs. Altogether, the results provide a thorough biophysical understanding of the nanodisc as a model membrane system, which is important in order to carry out and interpret experiments on membrane proteins embedded in such systems.

AB - Nanodiscs based on membrane scaffold proteins (MSPs) and phospholipids are used as membrane mimics to stabilize membrane proteins in solution for structural and functional studies. Combining small-angle X-ray scattering (SAXS), differential scanning calorimetry (DSC), and time-resolved small-angle neutron scattering (TR-SANS), we characterized the structure and lipid bilayer properties of five different nanodiscs made with dimyristoylphosphatidylcholine and different MSPs varying in size, charge, and circularization. Our SAXS modeling showed that the structural parameters of the embedded lipids are all similar, irrespective of the MSP properties. DSC showed that the lipid packing is not homogeneous in the nanodiscs and that a 20 Å wide boundary layer of lipids with perturbed packing is located close to the MSP, while the packing of central lipids is tighter than in large unilamellar vesicles. Finally, TR-SANS showed that lipid exchange rates in nanodiscs decrease with increasing nanodisc size and are lower for the nanodiscs made with supercharged MSPs compared to conventional nanodiscs. Altogether, the results provide a thorough biophysical understanding of the nanodisc as a model membrane system, which is important in order to carry out and interpret experiments on membrane proteins embedded in such systems.

U2 - 10.1021/acs.langmuir.1c00560

DO - 10.1021/acs.langmuir.1c00560

M3 - Journal article

C2 - 34038130

AN - SCOPUS:85108021041

VL - 37

SP - 6681

EP - 6690

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 22

ER -

ID: 274115184