Structural Reorganization of Cell Membrane Models Caused by the Anticancer Antibiotic Doxorubicin

N. N. Novikova; Новикова Н. Н.; M. V. Kovalchuk; Ковальчук М. В.; A. V. Rogachev; Рогачев А. В.; Yu. N. Malakhova; Малахова Ю. Н.; Yu. O. Kotova; Котова Ю. О.; S. E. Gelperina; Гельперина С. Э.; S. N. Yakunin; Якунин С. Н.

doi:10.31857/S0023476123600842

Structural Reorganization of Cell Membrane Models Caused by the Anticancer Antibiotic Doxorubicin

作者: Novikova N.N.¹, Kovalchuk M.V.¹, Rogachev A.V.¹, Malakhova Y.N.¹^,2, Kotova Y.O.³, Gelperina S.E.³, Yakunin S.N.¹
隶属关系:
1. National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
2. MIREA—Rusian Technological University, Moscow, Russia
3. Mendeleev University of Chemical Technology, 125047, Moscow, Russia
期: 卷 68, 编号 6 (2023)
页面: 990-1001
栏目: ПОВЕРХНОСТЬ, ТОНКИЕ ПЛЕНКИ
URL: https://jdigitaldiagnostics.com/0023-4761/article/view/673326
DOI: https://doi.org/10.31857/S0023476123600842
EDN: https://elibrary.ru/AAUWIR
ID: 673326

如何引用文章

全文:

开放存取

##reader.subscriptionAccessGranted##
受限制的访问

订阅存取

详细
作者简介
参考
补充文件
统计

详细

The molecular mechanisms of the interaction of anticancer antibiotic doxorubicin with lipid cell membrane models have been investigated using grazing incidence X-ray diffraction (XRD) and X-ray reflectivity (XRR). The model systems were monolayers of four types of phospholipids, related to the main components of animal cell membranes. New information on the processes of damage of phospholipid monolayer lattice caused by doxorubicin is obtained. It is established that the action of doxorubicin on anionic phospholipid monolayers is determined by the electrostatic interaction: positively charged doxorubicin molecules are incorporated between negatively charged phospholipid functional groups. In the case of neutral phospholipids the key role belongs to the hydrophobic interaction: doxorubicin molecules are coordinated with phospholipid hydrocarbon tails in disordered regions.

参考

Brezesinski G., Möhwald H. // Adv. Colloid Int. Sci. 2003. V. 100. P. 563. https://doi.org/10.1016/s0001-8686(02)00071-4
Stefaniu C., Brezesinski G. // Curr. Opin. Colloid Int. Sci. 2014. V. 19. P. 216. https://doi.org/10.1016/j.cocis.2014.01.004
Kaganer V.M., Mohwald H., Dutta P. // Rev. Modern Phys. 1999. V. 71. № 3. P. 779. https://doi.org/10.1103/RevModPhys.71.779
Daillant J., Gibaud A. X-ray and Neutron Reflectivity: Principles and Applications. Berlin: Springer, 2009. 348 p.
Новикова Н.Н., Ковальчук М.В., Юрьева Э.А. и др. // Кристаллография. 2012. Т. 57. № 5. С. 727.
Novikova N., Kovalchuk M., Konovalov O. et al. // BioNanoSci. 2021. V. 10. P. 618. https://doi.org/10.1007/s12668-020-00742-0
Arcamone F., Cassinelli G., Fantini G. et al. // Biotechnol. Bioeng. 2000. V. 67. P. 704. https://doi.org/10.1002/bit.260110607
Thorn C.F., Oshiro C., Marsh S. et al. // Pharmacogenet. Genomics. 2011. V. 21. P. 440. https://doi.org/10.1097/FPC.0b013e32833ffb56
Sritharan S., Sivalingam N.A. // Life Sci. 2021. V. 278. P. 119527. https://doi.org/10.1016/j.lfs.2021.119527
Asensio-L’opez M.C., Soler F., Pascual-Figal D. et al. // PLOS One. 2017. V. 12. P. e0172803. https://doi.org/10.1371/journal.pone.0172803
Alves A.C., Magarkar A., Horta M. et al. // Sci. Rep. 2017. V. 7. P. 6343. https://doi.org/10.1038/s41598-017-06445-z
Peetla C., Bhave R., Vijayaraghavalu S. et al. // Mol. Pharmaceutics. 2010. V. 7. P. 2334. https://doi.org/10.1021/mp100308n
Dadhich R., Kapoor S. // Mol. Cell. Biochem. 2022. V. 477. P. 2507. https://doi.org/10.1007/s11010-022-04459-4
Ramu A., Glaubiger D., Magrath I.T. et al. // Cancer Res. 1983. V. 43. P. 5533.
Speelmans G., Staffhorst R.W., de Kruijff B. et al. // Biochemistry. 1994. V. 33. P. 13761. https://doi.org/10.1021/bi00250a029
Chen L., Alrbyawi H., Poudel I. et al. // AAPS PharmSciTech. 2019. V. 20. P. 99. https://doi.org/10.1208/s12249-019-1316-0
Alves A., Nunes C., Lima J. et al. // Colloids Surf. B. 2017. V. 160. P. 610. https://doi.org/10.1016/j.colsurfb.2017.09.058
Yacoub T.J., Reddy A.S., Szleifer I. // Biophys. J. 2011. V. 101. P. 378. https://doi.org/10.1016/j.bpj.2011.06.015
Hou Y., Li J., Liu X. et al. // Chem. Phys. 2021. V. 541. P. 111036.
Matyszewska D., Moczulska S. // Electrochim. Acta. 2018. V. 280. P. 229. https://doi.org/10.1016/j.electacta.2018.05.119
Gaber M.H., Ghannam M.M., Ali S.A. et al. // Biophys. Chem. 1998. V. 70. P. 223. https://doi.org/10.1016/S0301-4622(97)00125-7
Marsh D. // Biochim. Biophys. Acta. 1996. V. 1286. P. 183. https://doi.org/10.1016/S0304-4157(96)00009-3
Zameshin A., Makhotkin I.A., Yakunin S.N. et al. // J. Appl. Cryst. 2016. V. 49. P. 1300. https://doi.org/10.1107/S160057671601044X
Kondratev O.A., Makhotkin I.A., Yakunin S.N. // Appl. Surf. Sci. 2022. V. 574. P. 151573. https://doi.org/10.1016/j.apsusc.2021.151573
Malakhova Y.N., Korovin A.N., Lapkin D.A. et al. // Soft Matter. 2017. V. 13. P. 7300. https://doi.org/10.1039/c7sm01773a
Windt D.L. // Comput. Phys. IEEE Comput. Sci. Eng. 1998. V. 12. P. 360. https://doi.org/10.1063/1.168689
Xiao-Lin Zh., Sow-Hsin Ch. // Phys. Rev. E. 1993. V. 47. P. 3174. https://doi.org/10.1103/PhysRevE.47.3174
Селеменев В.Ф., Рудакова Л.В., Рудаков О.Б. и др. Фосфолипиды на фоне природных матриц. Воронеж: Научная книга, 2020. 318 с.