Dataset Information

The antiarrhythmic compound efsevin directly modulates voltage-dependent anion channel 2 by binding to its inner wall and enhancing mitochondrial Ca²⁺ uptake.

ABSTRACT:

Background and purpose

The synthetic compound efsevin was recently identified to suppress arrhythmogenesis in models of cardiac arrhythmia, making it a promising candidate for antiarrhythmic therapy. Its activity was shown to be dependent on the voltage-dependent anion channel 2 (VDAC2) in the outer mitochondrial membrane. Here, we investigated the molecular mechanism of the efsevin-VDAC2 interaction.

Experimental approach

To evaluate the functional interaction of efsevin and VDAC2, we measured currents through recombinant VDAC2 in planar lipid bilayers. Using molecular ligand-protein docking and mutational analysis, we identified the efsevin binding site on VDAC2. Finally, physiological consequences of the efsevin-induced modulation of VDAC2 were analysed in HL-1 cardiomyoc

SUBMITTER: Wilting F

PROVIDER: S-EPMC7279994 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Dataset Information

The antiarrhythmic compound efsevin directly modulates voltage-dependent anion channel 2 by binding to its inner wall and enhancing mitochondrial Ca²⁺ uptake.

Background and purpose

Experimental approach

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

The antiarrhythmic compound efsevin directly modulates voltage-dependent anion channel 2 by binding to its inner wall and enhancing mitochondrial Ca2+ uptake.

Background and purpose

Experimental approach

OmicsDI is part of the ELIXIR infrastructure

Tweets

The antiarrhythmic compound efsevin directly modulates voltage-dependent anion channel 2 by binding to its inner wall and enhancing mitochondrial Ca²⁺ uptake.