Nitrated Fatty Acids Modulate the Physical Properties of Model Membranes and the Structure of Transmembrane Proteins

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  • Johannes Franz, Max Planck Institute for Polymer Research, Molecular Spectroscopy Department, 55128, Mainz, Germany., Institute for Pharmacy and Biochemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
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  • Tristan Bereau, Max Planck Institute for Polymer Research, Theory group, 55128, Mainz, Germany.
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  • Stefanie Pannwitt, Institute for Pharmacy and Biochemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
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  • Veerappan Anbazhagan, Current address: School of Chemical and Biotechnology, SASTRA University, Thanjavur, 613401, Tamil Nadu, India., Institute for Pharmacy and Biochemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
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  • Alexander Lehr, Institute for Organic Chemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
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  • Udo Nubbemeyer, Institute for Organic Chemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
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  • Ulrich Dietz, Regerstrasse 1, 65193, Wiesbaden, Germany.
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  • Mischa Bonn, Max Planck Institute for Polymer Research, Molecular Spectroscopy Department, 55128, Mainz, Germany.
  • ,
  • Tobias Weidner
  • Dirk Schneider, Institute for Pharmacy and Biochemistry, Johannes Gutenberg University, 55128, Mainz, Germany.

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.

OriginalsprogEngelsk
TidsskriftChemistry: A European Journal
Vol/bind23
Nummer40
Sider (fra-til)9690-9697
Antal sider8
ISSN0947-6539
DOI
StatusUdgivet - 2017

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