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Daniel Otzen

Refolding of SDS-Unfolded Proteins by Nonionic Surfactants

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Refolding of SDS-Unfolded Proteins by Nonionic Surfactants. / Kaspersen, Jørn Døvling; Søndergaard, Anne; Madsen, Daniel Jhaf et al.

In: Biophysical Journal, Vol. 112, No. 8, 25.04.2017, p. 1609-1620.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Kaspersen, JD, Søndergaard, A, Madsen, DJ, Otzen, DE & Pedersen, JS 2017, 'Refolding of SDS-Unfolded Proteins by Nonionic Surfactants', Biophysical Journal, vol. 112, no. 8, pp. 1609-1620. https://doi.org/10.1016/j.bpj.2017.03.013

APA

Kaspersen, J. D., Søndergaard, A., Madsen, D. J., Otzen, D. E., & Pedersen, J. S. (2017). Refolding of SDS-Unfolded Proteins by Nonionic Surfactants. Biophysical Journal, 112(8), 1609-1620. https://doi.org/10.1016/j.bpj.2017.03.013

CBE

Kaspersen JD, Søndergaard A, Madsen DJ, Otzen DE, Pedersen JS. 2017. Refolding of SDS-Unfolded Proteins by Nonionic Surfactants. Biophysical Journal. 112(8):1609-1620. https://doi.org/10.1016/j.bpj.2017.03.013

MLA

Kaspersen, Jørn Døvling et al. "Refolding of SDS-Unfolded Proteins by Nonionic Surfactants". Biophysical Journal. 2017, 112(8). 1609-1620. https://doi.org/10.1016/j.bpj.2017.03.013

Vancouver

Kaspersen JD, Søndergaard A, Madsen DJ, Otzen DE, Pedersen JS. Refolding of SDS-Unfolded Proteins by Nonionic Surfactants. Biophysical Journal. 2017 Apr 25;112(8):1609-1620. doi: 10.1016/j.bpj.2017.03.013

Author

Kaspersen, Jørn Døvling ; Søndergaard, Anne ; Madsen, Daniel Jhaf et al. / Refolding of SDS-Unfolded Proteins by Nonionic Surfactants. In: Biophysical Journal. 2017 ; Vol. 112, No. 8. pp. 1609-1620.

Bibtex

@article{8524cd036b0e4a79b14e5bb6b2250ce8,
title = "Refolding of SDS-Unfolded Proteins by Nonionic Surfactants",
abstract = "The strong and usually denaturing interaction between anionic surfactants (AS) and proteins/enzymes has both benefits and drawbacks: for example, it is put to good use in electrophoretic mass determinations but limits enzyme efficiency in detergent formulations. Therefore, studies of the interactions between proteins and AS as well as nonionic surfactants (NIS) are of both basic and applied relevance. The AS sodium dodecyl sulfate (SDS) denatures and unfolds globular proteins under most conditions. In contrast, NIS such as octaethylene glycol monododecyl ether (C12E8) and dodecyl maltoside (DDM) protect bovine serum albumin (BSA) from unfolding in SDS. Membrane proteins denatured in SDS can also be refolded by addition of NIS. Here, we investigate whether globular proteins unfolded by SDS can be refolded upon addition of C12E8 and DDM. Four proteins, BSA, α-lactalbumin (αLA), lysozyme, and β-lactoglobulin (βLG), were studied by small-angle x-ray scattering and both near- and far-UV circular dichroism. All proteins and their complexes with SDS were attempted to be refolded by the addition of C12E8, while DDM was additionally added to SDS-denatured αLA and βLG. Except for αLA, the proteins did not interact with NIS alone. For all proteins, the addition of NIS to the protein-SDS samples resulted in extraction of the SDS from the protein-SDS complexes and refolding of βLG, BSA, and lysozyme, while αLA changed to its NIS-bound state instead of the native state. We conclude that NIS competes with globular proteins for association with SDS, making it possible to release and refold SDS-denatured proteins by adding sufficient amounts of NIS, unless the protein also interacts with NIS alone.",
keywords = "Journal Article",
author = "Kaspersen, {J{\o}rn D{\o}vling} and Anne S{\o}ndergaard and Madsen, {Daniel Jhaf} and Otzen, {Daniel E} and Pedersen, {Jan Skov}",
note = "Copyright {\textcopyright} 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.",
year = "2017",
month = apr,
day = "25",
doi = "10.1016/j.bpj.2017.03.013",
language = "English",
volume = "112",
pages = "1609--1620",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Cell Press",
number = "8",

}

RIS

TY - JOUR

T1 - Refolding of SDS-Unfolded Proteins by Nonionic Surfactants

AU - Kaspersen, Jørn Døvling

AU - Søndergaard, Anne

AU - Madsen, Daniel Jhaf

AU - Otzen, Daniel E

AU - Pedersen, Jan Skov

N1 - Copyright © 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.

PY - 2017/4/25

Y1 - 2017/4/25

N2 - The strong and usually denaturing interaction between anionic surfactants (AS) and proteins/enzymes has both benefits and drawbacks: for example, it is put to good use in electrophoretic mass determinations but limits enzyme efficiency in detergent formulations. Therefore, studies of the interactions between proteins and AS as well as nonionic surfactants (NIS) are of both basic and applied relevance. The AS sodium dodecyl sulfate (SDS) denatures and unfolds globular proteins under most conditions. In contrast, NIS such as octaethylene glycol monododecyl ether (C12E8) and dodecyl maltoside (DDM) protect bovine serum albumin (BSA) from unfolding in SDS. Membrane proteins denatured in SDS can also be refolded by addition of NIS. Here, we investigate whether globular proteins unfolded by SDS can be refolded upon addition of C12E8 and DDM. Four proteins, BSA, α-lactalbumin (αLA), lysozyme, and β-lactoglobulin (βLG), were studied by small-angle x-ray scattering and both near- and far-UV circular dichroism. All proteins and their complexes with SDS were attempted to be refolded by the addition of C12E8, while DDM was additionally added to SDS-denatured αLA and βLG. Except for αLA, the proteins did not interact with NIS alone. For all proteins, the addition of NIS to the protein-SDS samples resulted in extraction of the SDS from the protein-SDS complexes and refolding of βLG, BSA, and lysozyme, while αLA changed to its NIS-bound state instead of the native state. We conclude that NIS competes with globular proteins for association with SDS, making it possible to release and refold SDS-denatured proteins by adding sufficient amounts of NIS, unless the protein also interacts with NIS alone.

AB - The strong and usually denaturing interaction between anionic surfactants (AS) and proteins/enzymes has both benefits and drawbacks: for example, it is put to good use in electrophoretic mass determinations but limits enzyme efficiency in detergent formulations. Therefore, studies of the interactions between proteins and AS as well as nonionic surfactants (NIS) are of both basic and applied relevance. The AS sodium dodecyl sulfate (SDS) denatures and unfolds globular proteins under most conditions. In contrast, NIS such as octaethylene glycol monododecyl ether (C12E8) and dodecyl maltoside (DDM) protect bovine serum albumin (BSA) from unfolding in SDS. Membrane proteins denatured in SDS can also be refolded by addition of NIS. Here, we investigate whether globular proteins unfolded by SDS can be refolded upon addition of C12E8 and DDM. Four proteins, BSA, α-lactalbumin (αLA), lysozyme, and β-lactoglobulin (βLG), were studied by small-angle x-ray scattering and both near- and far-UV circular dichroism. All proteins and their complexes with SDS were attempted to be refolded by the addition of C12E8, while DDM was additionally added to SDS-denatured αLA and βLG. Except for αLA, the proteins did not interact with NIS alone. For all proteins, the addition of NIS to the protein-SDS samples resulted in extraction of the SDS from the protein-SDS complexes and refolding of βLG, BSA, and lysozyme, while αLA changed to its NIS-bound state instead of the native state. We conclude that NIS competes with globular proteins for association with SDS, making it possible to release and refold SDS-denatured proteins by adding sufficient amounts of NIS, unless the protein also interacts with NIS alone.

KW - Journal Article

U2 - 10.1016/j.bpj.2017.03.013

DO - 10.1016/j.bpj.2017.03.013

M3 - Journal article

C2 - 28445752

VL - 112

SP - 1609

EP - 1620

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 8

ER -