Description
IBTP is a lipophilic cation that is accumulated in mitochondria and forms stable thioether adducts in a thiol-specific manner.
1 As a result, mitochondrial proteins that have changed thiol redox state following oxidative stress are selectively tagged with IBTP and can be separated by two-dimensional electrophoresis and isolated.
1 IBTP-tagged proteins can also be evaluated by immunoblotting using an antibody directed against the triphenylphosphonium moiety of the IBTP molecule.
2 IBTP has also been used as a mitochondria-targeted soft electrophile to inhibit mitochondrial oxidative phosphorylation.
3
References
1. Lin, T.-K., Hughes, G., Muratovska, A., et al.
Specific modification of mitochondrial protein thiols in response to oxidative stress: A proteomics approach J. Biol. Chem. 277(19),17048-17056(2002).
2. Venkatraman, A., Landar, A., Davis, A.J., et al.
Oxidative modification of hepatic mitochondria protein thiols: Effect of chronic alcohol consumption Am. J. Physiol. Gastrointest. Liver Physiol. 286(4),G521-G527(2004).
3. Vayalil, P.K., Oh, J.-Y., Zhou, F., et al.
A novel class of mitochondria-targeted soft electrophiles modifies mitochondrial proteins and inhibits mitochondrial metabolism in breast cancer cells through redox mechanisms PLoS One 10(3),(2015).
