Journal
FEBS LETTERS
Volume 588, Issue 10, Pages 1955-1960Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2014.04.004
Keywords
Outer membrane protein; OmpA; Surfactant; Biosurfactant; Rhamnolipid; Folding
Funding
- The Danish Council for Independent Research | Technology and Production Sciences
- Danish Research Foundation (inSPIN)
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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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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