Interaction between Iron Nitrosyl Complexes and Phosphatidylcholine Membranes: A Fluorescence Study

D. A. Poletaeva; Полетаева Д. А.; I. I. Faingold; Файнгольд И. И.; Yu. V. Soldatova; Солдатова Ю. В.; A. V. Smolina; Смолина А. В.; M. A. Savushkin; Савушкин М. А.; N. A. Sanina; Санина Н. А.; S. M. Aldoshin; Алдошин С. М.

doi:10.31857/S0044453723050217

Interaction between Iron Nitrosyl Complexes and Phosphatidylcholine Membranes: A Fluorescence Study

Autores: Poletaeva D.A.¹, Faingold I.I.¹, Soldatova Y.V.¹, Smolina A.V.¹, Savushkin M.A.², Sanina N.A.¹^,3, Aldoshin S.M.¹
Afiliações:
1. Federal Research Center of Problems of Chemical Physics and Medicinal Chemistry, Russian Academy of Sciences
2. Faculty of Chemistry, Moscow State University
3. Medicinal Chemistry Research and Educational Center
Edição: Volume 97, Nº 5 (2023)
Páginas: 617-623
Seção: ФИЗИКА И ХИМИЯ ЭЛЕМЕНТАРНЫХ ХИМИЧЕСКИХ ПРОЦЕССОВ
##submission.dateSubmitted##: 15.10.2023
##submission.datePublished##: 01.05.2023
URL: https://ogarev-online.ru/0044-4537/article/view/136567
DOI: https://doi.org/10.31857/S0044453723050217
EDN: https://elibrary.ru/HLWJUG
ID: 136567

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Resumo

Fluorescent probes: 8-anilino-1-naphthalenesulfonate (ANS), eosin Y, and pyrene were used to study the interaction between liposomes and three nitrosyl iron complexes that are promising anti-inflammatory agents and cardioprotectors. It was shown that the studied complexes compete with ANS molecules for the bonding sites in a bilayer of liposomes. The incorporation of the complexes into the lipid bilayer was also studied according to the quenching of eosin Y and pyrene fluorescence. The data suggest that iron nitrosyl complexes interact with the phospholipids headgroups and can penetrate deeper into the hydrophobic center of a lipid bilayer, where they affect the packing of fatty acid chains. The pronounced membranotropic properties of the complexes correlated with their ability to inhibit lipid peroxidation. Complexes with high constants of pyrene bonding are the most effective antioxidants.

Palavras-chave

nitrosyl iron complexes, NO donors, membrane liposomes, fluorescent probes, lipid peroxidation

Bibliografia

Vanin A.F. // Nitric Oxide. 2009. № 1 (21). C. 1–13. https://doi.org/10.1016/j.niox.2009.03.005
Sanina N.A., Aldoshin S.M., Shmatko N.Y. et al. // Inorganic Chemistry Comm. 2014. (49). C. 44. https://doi.org/10.1016/j.inoche.2014.09.016
Sanina N.A., Isaeva Y.A., Utenyshev A.N. et al. // Inorganica Chimica Acta. 2021. (527). C. 120559. https://doi.org/10.1016/j.ica.2021.120559
Sanina N.A., Aldoshin S.M., Shmatko N.Y. et al. // New Journal of Chemistry. 2015. № 2 (39). C. 1022. https://doi.org/10.1039/C4NJ01693A
Haynes D.H., Staerk H. // The Journal of Membrane Biology. 1974. № 1 (17). C. 313. https://doi.org/10.1007/BF01870190
Ma J.Y., Ma J.K., Weber K.C. // Journal of Lipid Research. 1985. № 6 (26). C. 735–744. https://doi.org/10.1016/S0022-2275(20)34331-5
Rooijen N. Van, Sanders A. // Journal of Immunological Methods. 1994. № 1–2 (174). C. 83. https://doi.org/10.1016/0022-1759(94)90012-4
Montero M.T., Pijoan M., Merino-Montero S. et al. // Langmuir. 2006. № 18 (22). C. 7574. https://doi.org/10.1021/la060633c
Haynes D.H. // The Journal of Membrane Biology. 1974. № 1 (17). C. 341. https://doi.org/10.1007/BF01870191
Hughes Z.E., Mark A.E., Mancera R.L. // The Journal of Physical Chemistry B. 2012. № 39 (116). C. 11911. https://doi.org/10.1021/jp3035538
Sanina N.A., Sulimenkov I.V., Emel’yanova N.S. et al. // Dalton Transactions. 2022. № 22 (51). C. 8893–8905. https://doi.org/10.1039/D2DT01011A
Cevc G. // Biochimica et Biophysica Acta (BBA) – Reviews on Biomembranes. 1990. № 3 (1031). C. 311–382. https://doi.org/10.1016/0304-4157(90)90015-5
Lakowicz J.R. Ed. Principles of Fluorescence Spectroscopy. Boston, MA: Springer US, 2006. ISBN: 978-0-387-31278-1.
Podo F., Blasie J.K. // Proceedings of the National Academy of Sciences of the United States of America. 1977. № 3 (74). P. 1032.
Förster T., Kasper K. // Zeitschrift für Elektrochemie, Berichte der Bunsengesellschaft für Physikalische Chemie. 1955. № 10 (59). C. 976.
Mclean L., Hagaman K. // Free Radical Biology and Medicine. 1992. № 2(12). C. 113. https://doi.org/10.1016/0891-5849(92)90004-Z
Hinzmann J.S., McKenna R.L., Pierson T.S. et al. // Chemistry and Physics of Lipids. 1992. № 2 (62). C. 123. https://doi.org/10.1016/0009-3084(92)90090-C
Audus K.L., Guillot F.L., Mark Braughler J. // Free Radical Biology and Medicine. 1991. № 4 (11). C. 361. https://doi.org/10.1016/0891-5849(91)90152-S
McLean L.R., Hagaman K.A. // Biochemistry. 1989. № 1 (28). C. 321. https://doi.org/10.1021/bi00427a043
Dache T.C., Motta C., Neufcour D., Jacotot B. // Journal of Clinical Biochemistry and Nutrition. 1991. № 1 (10). C. 51. https://doi.org/10.3164/jcbn.10.51
Fukuzawa K., Chida H., Tokumura A., Tsukatani H. // Archives of Biochemistry and Biophysics. 1981. № 1 (206). C. 173. https://doi.org/10.1016/0003-9861(81)90078-3
Urano S., Inomori Y., Sugawara T. et al. // Journal of Biological Chemistry. 1992. № 26 (267). C. 18365. https://doi.org/10.1016/S0021-9258(19)36970-4
Suzuki Y.J., Tsuchiya M., Wassall S.R. et al. // Biochemistry. 1993. № 40 (32). C. 10692. https://doi.org/10.1021/bi00091a020
Valko M., Leibfritz D., Moncol J. et al. // The International Journal of Biochemistry & Cell Biology. 2007. № 1 (39). C. 44. https://doi.org/10.1016/j.biocel.2006.07.001
Hummel S.G., Fischer A.J., Martin S.M. et al. // Free Radical Biology and Medicine. 2006. № 3 (40). C. 501. https://doi.org/10.1016/j.freeradbiomed.2005.08.047