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Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid

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Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. / Andersen, Kell K; Otzen, Daniel.

In: FEBS Letters, Vol. 588, No. 10, 21.05.2014, p. 1955-1960.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Andersen, KK & Otzen, D 2014, 'Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid', FEBS Letters, vol. 588, no. 10, pp. 1955-1960. https://doi.org/10.1016/j.febslet.2014.04.004

APA

Andersen, K. K., & Otzen, D. (2014). Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. FEBS Letters, 588(10), 1955-1960. https://doi.org/10.1016/j.febslet.2014.04.004

CBE

Andersen KK, Otzen D. 2014. Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. FEBS Letters. 588(10):1955-1960. https://doi.org/10.1016/j.febslet.2014.04.004

MLA

Andersen, Kell K and Daniel Otzen. "Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid". FEBS Letters. 2014, 588(10). 1955-1960. https://doi.org/10.1016/j.febslet.2014.04.004

Vancouver

Andersen KK, Otzen D. Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. FEBS Letters. 2014 May 21;588(10):1955-1960. doi: 10.1016/j.febslet.2014.04.004

Author

Andersen, Kell K ; Otzen, Daniel. / Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. In: FEBS Letters. 2014 ; Vol. 588, No. 10. pp. 1955-1960.

Bibtex

@article{7bbe05dcdaf7405581e2e0f08fe2d14c,
title = "Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid",
abstract = "Folding and stability of bacterial outer membrane proteins (OMPs) are typically studied in vitro using model systems such as phospholipid vesicles or surfactant. OMP folding requires surfactant concentrations above the critical micelle concentration (cmc) and usually only occurs in neutral or zwitterionic surfactants, but not in anionic or cationic surfactants. Various Gram-negative bacteria produce the anionic biosurfactant rhamnolipid. Here we show that the OMP OmpA can be folded in rhamnolipid at concentrations above the cmc, though the thermal stability is reduced compared to the non-ionic surfactant dodecyl maltoside. We discuss implications for possible interactions between OMPs and biosurfactants in vivo.",
author = "Andersen, {Kell K} and Daniel Otzen",
note = "Copyright {\textcopyright} 2014. Published by Elsevier B.V.",
year = "2014",
month = may,
day = "21",
doi = "10.1016/j.febslet.2014.04.004",
language = "English",
volume = "588",
pages = "1955--1960",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
number = "10",

}

RIS

TY - JOUR

T1 - Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid

AU - Andersen, Kell K

AU - Otzen, Daniel

N1 - Copyright © 2014. Published by Elsevier B.V.

PY - 2014/5/21

Y1 - 2014/5/21

N2 - Folding and stability of bacterial outer membrane proteins (OMPs) are typically studied in vitro using model systems such as phospholipid vesicles or surfactant. OMP folding requires surfactant concentrations above the critical micelle concentration (cmc) and usually only occurs in neutral or zwitterionic surfactants, but not in anionic or cationic surfactants. Various Gram-negative bacteria produce the anionic biosurfactant rhamnolipid. Here we show that the OMP OmpA can be folded in rhamnolipid at concentrations above the cmc, though the thermal stability is reduced compared to the non-ionic surfactant dodecyl maltoside. We discuss implications for possible interactions between OMPs and biosurfactants in vivo.

AB - Folding and stability of bacterial outer membrane proteins (OMPs) are typically studied in vitro using model systems such as phospholipid vesicles or surfactant. OMP folding requires surfactant concentrations above the critical micelle concentration (cmc) and usually only occurs in neutral or zwitterionic surfactants, but not in anionic or cationic surfactants. Various Gram-negative bacteria produce the anionic biosurfactant rhamnolipid. Here we show that the OMP OmpA can be folded in rhamnolipid at concentrations above the cmc, though the thermal stability is reduced compared to the non-ionic surfactant dodecyl maltoside. We discuss implications for possible interactions between OMPs and biosurfactants in vivo.

U2 - 10.1016/j.febslet.2014.04.004

DO - 10.1016/j.febslet.2014.04.004

M3 - Journal article

C2 - 24735722

VL - 588

SP - 1955

EP - 1960

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 10

ER -