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FEBS Lett. 2014 May 21;588(10):1955-60. doi: 10.1016/j.febslet.2014.04.004. Epub 2014 Apr 13.

Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid.

Author information

1
iNANO, Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 14, DK - 8000 Aarhus C, Denmark. Electronic address: kell.andersen@inano.au.dk.
2
iNANO, Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 14, DK - 8000 Aarhus C, Denmark. Electronic address: dao@inano.au.dk.

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.

KEYWORDS:

Biosurfactant; Folding; OmpA; Outer membrane protein; Rhamnolipid; Surfactant

PMID:
24735722
DOI:
10.1016/j.febslet.2014.04.004
[Indexed for MEDLINE]
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