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Nitrated Fatty Acids Modulate the Physical Properties of Model Membranes and the Structure of Transmembrane Proteins.
Franz, Johannes; Bereau, Tristan; Pannwitt, Stefanie; Anbazhagan, Veerappan; Lehr, Alexander; Nubbemeyer, Udo; Dietz, Ulrich; Bonn, Mischa; Weidner, Tobias; Schneider, Dirk.
Afiliação
  • Franz J; Institute for Pharmacy and Biochemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
  • Bereau T; Max Planck Institute for Polymer Research, Molecular Spectroscopy Department, 55128, Mainz, Germany.
  • Pannwitt S; Max Planck Institute for Polymer Research, Theory group, 55128, Mainz, Germany.
  • Anbazhagan V; Institute for Pharmacy and Biochemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
  • Lehr A; Institute for Pharmacy and Biochemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
  • Nubbemeyer U; Current address: School of Chemical and Biotechnology, SASTRA University, Thanjavur, 613401, Tamil Nadu, India.
  • Dietz U; Institute for Organic Chemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
  • Bonn M; Institute for Organic Chemistry, Johannes Gutenberg University, 55128, Mainz, Germany.
  • Weidner T; Regerstrasse 1, 65193, Wiesbaden, Germany.
  • Schneider D; Max Planck Institute for Polymer Research, Molecular Spectroscopy Department, 55128, Mainz, Germany.
Chemistry ; 23(40): 9690-9697, 2017 Jul 18.
Article em En | MEDLINE | ID: mdl-28504864
ABSTRACT
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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Membrana Celular / Ácidos Graxos / Proteínas de Membrana / Nitratos Idioma: En Revista: Chemistry Assunto da revista: QUIMICA Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Membrana Celular / Ácidos Graxos / Proteínas de Membrana / Nitratos Idioma: En Revista: Chemistry Assunto da revista: QUIMICA Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Alemanha