The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane Organization
The mechanism of the interaction of highly hydroxylated fullerenol C60(OH)36 with erythrocyte membranes was studied by electron spin resonance spectroscopy (ESR) of stearic acid derivatives labeled with a nitroxyl radical at C-12 or C-16 and with a nitroxyl derivative of maleimide covalently attache...
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| Format: | Article |
| Language: | English |
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Wiley
2015-01-01
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| Series: | Journal of Spectroscopy |
| Online Access: | http://dx.doi.org/10.1155/2015/825914 |
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| author | Jacek Grebowski Anita Krokosz |
| author_facet | Jacek Grebowski Anita Krokosz |
| author_sort | Jacek Grebowski |
| collection | DOAJ |
| description | The mechanism of the interaction of highly hydroxylated fullerenol C60(OH)36 with erythrocyte membranes was studied by electron spin resonance spectroscopy (ESR) of stearic acid derivatives labeled with a nitroxyl radical at C-12 or C-16 and with a nitroxyl derivative of maleimide covalently attached to sulfhydryl groups of membrane proteins. A significant increase in membrane fluidity in the hydrophobic region of the lipid bilayer was observed for 12-doxylstearic acid at fullerenol concentrations of 100 mg/L or 150 mg/L, while for 16-doxylstearic acid significant increase in fluidity was only observed at 150 mg/L. Fullerenol at 100 mg/L or 150 mg/L caused conformational changes in membrane proteins, expressed as an increase in the hw/hs parameter, when fullerenol was added before the maleimide spin label (MSL) to the membrane suspension. The increase of the hw/hs parameter may be caused by changes in lipid-protein or protein-protein interactions which increase the mobility of the MSL label and as a result increase the membrane fluidity. Incubation of the membranes with the MSL before the addition of fullerenol blocked the available membrane protein –SH groups and minimized the interaction of fullerenol with them. This confirms that fullerenol interacts with erythrocyte membrane proteins via available protein –SH groups. |
| format | Article |
| id | doaj-art-4909e66ce4ed4edfa94316fbdff57b07 |
| institution | Kabale University |
| issn | 2314-4920 2314-4939 |
| language | English |
| publishDate | 2015-01-01 |
| publisher | Wiley |
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| series | Journal of Spectroscopy |
| spelling | doaj-art-4909e66ce4ed4edfa94316fbdff57b072025-02-03T05:51:32ZengWileyJournal of Spectroscopy2314-49202314-49392015-01-01201510.1155/2015/825914825914The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane OrganizationJacek Grebowski0Anita Krokosz1Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, 141/143 Pomorska Street, 90-236 Lodz, PolandDepartment of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, 141/143 Pomorska Street, 90-236 Lodz, PolandThe mechanism of the interaction of highly hydroxylated fullerenol C60(OH)36 with erythrocyte membranes was studied by electron spin resonance spectroscopy (ESR) of stearic acid derivatives labeled with a nitroxyl radical at C-12 or C-16 and with a nitroxyl derivative of maleimide covalently attached to sulfhydryl groups of membrane proteins. A significant increase in membrane fluidity in the hydrophobic region of the lipid bilayer was observed for 12-doxylstearic acid at fullerenol concentrations of 100 mg/L or 150 mg/L, while for 16-doxylstearic acid significant increase in fluidity was only observed at 150 mg/L. Fullerenol at 100 mg/L or 150 mg/L caused conformational changes in membrane proteins, expressed as an increase in the hw/hs parameter, when fullerenol was added before the maleimide spin label (MSL) to the membrane suspension. The increase of the hw/hs parameter may be caused by changes in lipid-protein or protein-protein interactions which increase the mobility of the MSL label and as a result increase the membrane fluidity. Incubation of the membranes with the MSL before the addition of fullerenol blocked the available membrane protein –SH groups and minimized the interaction of fullerenol with them. This confirms that fullerenol interacts with erythrocyte membrane proteins via available protein –SH groups.http://dx.doi.org/10.1155/2015/825914 |
| spellingShingle | Jacek Grebowski Anita Krokosz The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane Organization Journal of Spectroscopy |
| title | The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane Organization |
| title_full | The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane Organization |
| title_fullStr | The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane Organization |
| title_full_unstemmed | The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane Organization |
| title_short | The Effect of Highly Hydroxylated Fullerenol C60(OH)36 on Human Erythrocyte Membrane Organization |
| title_sort | effect of highly hydroxylated fullerenol c60 oh 36 on human erythrocyte membrane organization |
| url | http://dx.doi.org/10.1155/2015/825914 |
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