Self-assembling peptides form nanodiscs that stabilize membrane proteins

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Self-assembling peptides form nanodiscs that stabilize membrane proteins. / Midtgaard, Søren Roi; Pedersen, Martin Cramer; Kirkensgaard, Jacob Judas Kain; Sørensen, Kasper Kildegaard; Mortensen, Kell; Jensen, Knud Jørgen; Arleth, Lise.

In: Soft Matter, Vol. 10, No. 5, 01.01.2014, p. 738-752.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Midtgaard, SR, Pedersen, MC, Kirkensgaard, JJK, Sørensen, KK, Mortensen, K, Jensen, KJ & Arleth, L 2014, 'Self-assembling peptides form nanodiscs that stabilize membrane proteins', Soft Matter, vol. 10, no. 5, pp. 738-752. https://doi.org/10.1039/c3sm51727f

APA

Midtgaard, S. R., Pedersen, M. C., Kirkensgaard, J. J. K., Sørensen, K. K., Mortensen, K., Jensen, K. J., & Arleth, L. (2014). Self-assembling peptides form nanodiscs that stabilize membrane proteins. Soft Matter, 10(5), 738-752. https://doi.org/10.1039/c3sm51727f

Vancouver

Midtgaard SR, Pedersen MC, Kirkensgaard JJK, Sørensen KK, Mortensen K, Jensen KJ et al. Self-assembling peptides form nanodiscs that stabilize membrane proteins. Soft Matter. 2014 Jan 1;10(5):738-752. https://doi.org/10.1039/c3sm51727f

Author

Midtgaard, Søren Roi ; Pedersen, Martin Cramer ; Kirkensgaard, Jacob Judas Kain ; Sørensen, Kasper Kildegaard ; Mortensen, Kell ; Jensen, Knud Jørgen ; Arleth, Lise. / Self-assembling peptides form nanodiscs that stabilize membrane proteins. In: Soft Matter. 2014 ; Vol. 10, No. 5. pp. 738-752.

Bibtex

@article{e069a26d1a1046a3baad738069340a2c,
title = "Self-assembling peptides form nanodiscs that stabilize membrane proteins",
abstract = "New methods to handle membrane bound proteins, e.g. G-protein coupled receptors (GPCRs), are highly desirable. Recently, apoliprotein A1 (ApoA1) based lipoprotein particles have emerged as a new platform for studying membrane proteins, and it has been shown that they can self-assemble in combination with phospholipids to form discoidal shaped particles that can stabilize membrane proteins. In the present study, we have investigated an ApoA1 mimetic peptide with respect to its solution structure when in complex with phospholipids. This was achieved using a powerful combination of small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) supported by coarse-grained molecular dynamics simulations. The detailed structure of the discs was determined in unprecedented detail and it was found that they adopt a discoidal structure very similar to the ApoA1 based nanodiscs. We furthermore show that, like the ApoA1 and derived nanodiscs, these peptide discs can accommodate and stabilize a membrane protein. Finally, we exploit their dynamic properties and show that the 18A discs may be used for transferring membrane proteins and associated phospholipids directly and gently into phospholipid nanodiscs.",
author = "Midtgaard, {S{\o}ren Roi} and Pedersen, {Martin Cramer} and Kirkensgaard, {Jacob Judas Kain} and S{\o}rensen, {Kasper Kildegaard} and Kell Mortensen and Jensen, {Knud J{\o}rgen} and Lise Arleth",
year = "2014",
month = "1",
day = "1",
doi = "10.1039/c3sm51727f",
language = "English",
volume = "10",
pages = "738--752",
journal = "Soft Matter",
issn = "1744-683X",
publisher = "Royal Society of Chemistry",
number = "5",

}

RIS

TY - JOUR

T1 - Self-assembling peptides form nanodiscs that stabilize membrane proteins

AU - Midtgaard, Søren Roi

AU - Pedersen, Martin Cramer

AU - Kirkensgaard, Jacob Judas Kain

AU - Sørensen, Kasper Kildegaard

AU - Mortensen, Kell

AU - Jensen, Knud Jørgen

AU - Arleth, Lise

PY - 2014/1/1

Y1 - 2014/1/1

N2 - New methods to handle membrane bound proteins, e.g. G-protein coupled receptors (GPCRs), are highly desirable. Recently, apoliprotein A1 (ApoA1) based lipoprotein particles have emerged as a new platform for studying membrane proteins, and it has been shown that they can self-assemble in combination with phospholipids to form discoidal shaped particles that can stabilize membrane proteins. In the present study, we have investigated an ApoA1 mimetic peptide with respect to its solution structure when in complex with phospholipids. This was achieved using a powerful combination of small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) supported by coarse-grained molecular dynamics simulations. The detailed structure of the discs was determined in unprecedented detail and it was found that they adopt a discoidal structure very similar to the ApoA1 based nanodiscs. We furthermore show that, like the ApoA1 and derived nanodiscs, these peptide discs can accommodate and stabilize a membrane protein. Finally, we exploit their dynamic properties and show that the 18A discs may be used for transferring membrane proteins and associated phospholipids directly and gently into phospholipid nanodiscs.

AB - New methods to handle membrane bound proteins, e.g. G-protein coupled receptors (GPCRs), are highly desirable. Recently, apoliprotein A1 (ApoA1) based lipoprotein particles have emerged as a new platform for studying membrane proteins, and it has been shown that they can self-assemble in combination with phospholipids to form discoidal shaped particles that can stabilize membrane proteins. In the present study, we have investigated an ApoA1 mimetic peptide with respect to its solution structure when in complex with phospholipids. This was achieved using a powerful combination of small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) supported by coarse-grained molecular dynamics simulations. The detailed structure of the discs was determined in unprecedented detail and it was found that they adopt a discoidal structure very similar to the ApoA1 based nanodiscs. We furthermore show that, like the ApoA1 and derived nanodiscs, these peptide discs can accommodate and stabilize a membrane protein. Finally, we exploit their dynamic properties and show that the 18A discs may be used for transferring membrane proteins and associated phospholipids directly and gently into phospholipid nanodiscs.

U2 - 10.1039/c3sm51727f

DO - 10.1039/c3sm51727f

M3 - Journal article

C2 - 24651399

AN - SCOPUS:84891715038

VL - 10

SP - 738

EP - 752

JO - Soft Matter

JF - Soft Matter

SN - 1744-683X

IS - 5

ER -

ID: 130691074