Email this article Molecular dynamics modeling of the interaction of cationic fluorescent lipid peroxidation-sensitive probes with the mitochondrial membrane
- Authors: Nesterenko A.M.1,2, Kholina E.G.3, Lyamzaev K.G.1, Mulkidzhanyan A.Y.1,3,4, Chernyak B.V.1
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Affiliations:
- A.N. Belozersky Institute of physico-chemical biology, Moscow State University
- Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences
- Lomonosov Moscow State University
- Osnabrück University
- Issue: Vol 486, No 4 (2019)
- Pages: 509-513
- Section: Biochemistry, biophysics, molecular biology
- URL: https://journals.eco-vector.com/0869-5652/article/view/14481
- DOI: https://doi.org/10.31857/S0869-56524864509-513
- ID: 14481
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Abstract
Cardiolipin (CL) plays a central role in lipid peroxidation (LPO) of the mitochondrial inner membrane due to higher content of unsaturated fatty acids in CL in comparison with the other phospholipids. CL oxidation plays an important role in the regulation of various intracellular signaling pathways and its excessive oxidation contributes to the development of various pathologies and, possibly, participates in the aging process. Mitochondria-targeted antioxidants containing triphenylphosphonium cation (TPP+) effectively protect CL from oxidation. It is assumed that fluorescent probes on the basis of the C11-BODIPY fluorophore sensitive to LPO and containing TPP+ can selectively register CL oxidation. To test this possibility, we carried out a molecular dynamic simulation of such probes in a model mitochondrial membrane. It is shown that the probes are located in the membrane at the same depth as the unsaturated bonds in CL molecules sensitive to oxidation. Increasing the length of the linker that binds the fluorophore and TPP+ residue has little effect on the position of the probe in the membrane. This indicates the possibility of modifying the linker to increase the selectivity of the probes to CL.
About the authors
A. M. Nesterenko
A.N. Belozersky Institute of physico-chemical biology, Moscow State University; Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences
Email: bchernyak@yahoo.com
Russian Federation, 40, Leninskie gory, 1, bld, Moscow , 119992; 16/10, Miklukho-Maklaya Street, Moscow, 117997
E. G. Kholina
Lomonosov Moscow State University
Email: bchernyak@yahoo.com
Russian Federation, 1, Leninskie gory, Moscow, 119991
K. G. Lyamzaev
A.N. Belozersky Institute of physico-chemical biology, Moscow State University
Email: bchernyak@yahoo.com
Russian Federation, 40, Leninskie gory, 1, bld, Moscow , 119992
A. Y. Mulkidzhanyan
A.N. Belozersky Institute of physico-chemical biology, Moscow State University; Lomonosov Moscow State University; Osnabrück University
Email: bchernyak@yahoo.com
Russian Federation, A.N. Belozersky Institute of physico-chemical biology, Moscow State University; 1, Leninskie gory, Moscow, 119991; 30, Albrechtschrasse, Osnabruck, Germany, 49076
B. V. Chernyak
A.N. Belozersky Institute of physico-chemical biology, Moscow State University
Author for correspondence.
Email: bchernyak@yahoo.com
Russian Federation, 40, Leninskie gory, 1, bld, Moscow , 119992
References
- Zorov D.B., Juhaszova M., Sollott S.J. // Physiol Rev. 2014. V. 94. № 3. P. 909-950.
- Maguire J.J., Tyurina Y.Y., Mohammadyani D., Kapralov A.A., Anthonymuthu T.S., Qu F., Amoscato A.A., Sparvero L.J., Tyurin V.A., Planas-Iglesias J., He R.R., Klein-Seetharaman J., Bayır H, Kagan V.E. // Biochim. Biophys. Acta.-Mol. Cell. Biol. Lipids. 2017. V. 1862. № 1. P. 8-24.
- Kagan V.E., Bayir H.A., Belikova N.A., Kapralov O., Tyurina Y.Y., Tyurin V.A., Jiang J., Stoyanovsky D.A., Wipf P., Kochanek P.M., Greenberger J.S., Pitt B., Shvedova A.A., Borisenko G. // Free Radic. Biol. Med. 2009. V. 46. № 11. P. 1439-1453.
- Skulachev V.P., Antonenko Y.N., Cherepanov D.A., Chernyak B.V., Izyumov D.S., Khailova L.S., Klishin S.S., Korshunova G.A., Lyamzaev K.G., Pletjushkina O.Y., Roginsky V.A., Rokitskaya T.I., Severin F.F., Severina I.I., Simonyan R.A., Skulachev M.V., Sumbatyan N.V., Sukhanova E.I., Tashlitsky V.N., Trendeleva T.A., Vyssokikh M.Y., Zvyagilskaya R.A. // Biochim. Biophys. Acta. 2010. V. 1797. № 6-7. P. 878-889.
- Lokhmatikov A.V., Voskoboynikova N., Cherepanov D.A., Skulachev M.V., Steinhoff H.J., Skulachev V.P., Mulkidjanian A.Y. // Oxid. Med. Cell. Longev. 2016. V. 2016. P. 8 679 469.
- Prime T.A., Forkink M., Logan A., Finichiu P.G., McLachlan J., Li Pun P.B., Koopman W.J., Larsen L., Latter M.J., Smith R.A., Murphy M.P. // Free Radic. Biol. Med. 2012. V. 53. № 3. P. 544-553.
- Drummen G.P., van Liebergen L.C., Op den Kamp J.A., Post J.A. // Free Radic. Biol. Med. 2002. V. 33. № 4. P. 473-90.
- Comte J., Maǐsterrena B., Gautheron D.C. // Biochim. Biophys. Acta - Biomembr. 1976. V. 419. № 2. P. 271-284.
- Klauda J.B., Venable R.M., Freites J.A., O’Connor J.W., Tobias D.J., Mondragon-Ramirez, C., Vorobyov I., MacKerell A., Pastor R.W. // J. Phys. Chem. B. 2010. V. 114. № 23. P. 7830-7843.
- Granovsky A.A. Firefly version 8, http://classic.chem.msu.su/gran/firefly/index.html
- Phan M.D., Shin K. // Biophys. J. 2015. V. 108. № 8. P. 1977-1986.
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