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Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid
Author(s) -
Andersen Kell K.,
Otzen Daniel E.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.04.004
Subject(s) - rhamnolipid , pulmonary surfactant , critical micelle concentration , chemistry , micelle , bacterial outer membrane , cationic polymerization , vesicle , folding (dsp implementation) , phospholipid , membrane , biophysics , chemical engineering , bacteria , organic chemistry , biochemistry , aqueous solution , escherichia coli , biology , pseudomonas aeruginosa , genetics , gene , electrical engineering , engineering
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 .