6533b821fe1ef96bd127c25a
RESEARCH PRODUCT
Nitrated Fatty Acids Modulate the Physical Properties of Model Membranes and the Structure of Transmembrane Proteins
Mischa BonnAlexander LehrTristan BereauUlrich DietzStefanie PannwittJohannes FranzJohannes FranzUdo NubbemeyerDirk SchneiderVeerappan AnbazhaganVeerappan AnbazhaganTobias Weidnersubject
inorganic chemicals0301 basic medicineProtein Conformationcomplex mixturesPhase TransitionCatalysisPhysical Phenomena03 medical and health sciences0302 clinical medicineProtein structureJournal ArticleFluorescence Resonance Energy TransferMembrane fluidityComputer SimulationLipid bilayerIntegral membrane proteinNitratesChemistryCircular DichroismCell MembraneFatty AcidsOrganic ChemistryPeripheral membrane proteinMembrane ProteinsGeneral Chemistryrespiratory systemLipidsTransmembrane protein030104 developmental biologyMembraneMembrane proteinBiochemistryBiophysics030217 neurology & neurosurgerySignal Transductiondescription
Nitrated fatty acids (NO2 -FAs) act as anti-inflammatory signal mediators, albeit the molecular mechanisms behind NO2 -FAs' influence on diverse metabolic and signaling pathways in inflamed tissues are essentially elusive. Here, we combine fluorescence measurements with surface-specific sum frequency generation vibrational spectroscopy and coarse-grained computer simulations to demonstrate that NO2 -FAs alter lipid organization by accumulation at the membrane-water interface. As the function of membrane proteins strongly depends on both, protein structure as well as membrane properties, we consecutively follow the structural dynamics of an integral membrane protein in presence of NO2 -FAs. Based on our results, we suggest a molecular mechanism of the NO2 -FA in vivo activity: Driven by the NO2 -FA-induced lipid layer reorganization, the structure and function of membrane-associated (signaling) proteins is indirectly affected.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2017-06-29 | Chemistry – A European Journal |