Binding of the immunomodulatory drug Bz-423 to mitochondrial FoF1-ATP synthase in living cells by FRET acceptor photobleaching

@inproceedings{Starke2016BindingOT,
  title={Binding of the immunomodulatory drug Bz-423 to mitochondrial FoF1-ATP synthase in living cells by FRET acceptor photobleaching},
  author={Ilka Starke and Kathryn Marie Johnson and Jan Petersen and Peter Gr{\"a}ber and Anthony Opipari and Gary D Glick and Michael B{\"o}rsch},
  booktitle={SPIE BiOS},
  year={2016}
}
Bz-423 is a promising new drug for treatment of autoimmune diseases. This small molecule binds to subunit OSCP of the mitochondrial enzyme FoF1-ATP synthase and modulates its catalytic activities. We investigate the binding of Bz-423 to mitochondria in living cells and how subunit rotation in FoF1-ATP synthase, i.e. the mechanochemical mechanism of this enzyme, is affected by Bz-423. Therefore, the enzyme was marked selectively by genetic fusion with the fluorescent protein EGFP to the C… 

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TLDR
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TLDR
Their mitochondrial nano-environment was investigated by FLIM and superresolution microscopy in living human cells and different lifetimes and anisotropy values were found.

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TLDR
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Towards monitoring conformational changes of the GPCR neurotensin receptor 1 by single-molecule FRET

TLDR
G protein-coupled receptor 1 was found to be monomeric in liposomes, with a small fraction being dimeric and oligomeric, showing homoFRET, and agonist binding to NTSR1 was demonstrated by time-resolved single-molecule Förster resonance energy transfer (smFRET), using neurotensin labeled with the fluorophore ATTO594.

Observing monomer: dimer transitions of neurotensin receptors 1 in single SMALPs by homoFRET and in an ABELtrap

TLDR
The oligomerization state of the human NTSR1 tagged with mRuby3 is reported by dissolving the plasma membranes of living HEK293T cells into 10 nm-sized soluble lipid nanoparticles by addition of styrene-maleic acid copolymers (SMALPs).

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