Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid

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

SN - 0014-5793

VL - 588

SP - 1955

EP - 1960

JO - FEBS Letters

JF - FEBS Letters

IS - 10

ER -