Interactions between antitumor alkylphosphocholines and membrane sphingolipids in Langmuir monolayers

2014
journal article
article
1
cris.lastimport.wos2024-04-09T19:01:05Z
dc.abstract.enAlkylphosphocholines (APCs) are new generation, highly selective antineoplastic drugs, whose mechanism of action is not fully understood. It is known that in contrast to traditional chemotherapeutics, APCs do not induce cell death by apoptosis or necrosis as a result of DNA damage, but target cellular membranes and affect their biophysical properties. However, it is still unknown which membrane component attracts APC molecules selectively to cancer cells. In order to get insight into this issue, systematic investigations on the interactions between APCs and particular membrane components are highly required. Such experiments can be performed with the Langmuir monolayer technique, serving as a biomembrane model. Because of overexpression of gangliosides in tumor progression and the ability of APCs to insert into membrane rafts, two sphingolipids, i.e. sphingomyelin (SM) and ganglioside GM1 have been examined as potential membrane targets. In this respect, their interactions with three alkylphosphocholines, differing in their hydrophobic part: hexadecylphosphocholine (HePC), octadecylphosphocholine (OcPC) and erucylphosphocholine (ErPC) have been studied and the following systems have been analysed: SM(or GM1)/HePC, SM(or GM1)/OcPC and SM(or GM1)/ErPC. It was found that all the investigated APCs show strong affinity to ganglioside in contrast to sphingomyelin. Differences in interaction of APCs with both investigated sphingolipids were studied based on experimental surface pressure ( \pi ) versus mean molecular area (A) isotherms, and analyzed qualitatively (with mean molecular area values) as well as quantitatively (with \Delta G^{exc} function). The obtained results have also been analysed taking into consideration geometry of interacting molecules. Our results suggest that gangliosides may be molecular targets for APCs, attracting them to tumor cells. Although the interactions with sphingomyelin were found to be unfavourable, further studies on more complex system, containing APCs mixed with sphingomyelin and cholesterol, are required to better understand the role of lipid rafts in the selectivity of APCs.pl
dc.affiliationWydział Chemii : Zakład Chemii Ogólnejpl
dc.affiliationWydział Fizyki, Astronomii i Informatyki Stosowanej : Instytut Fizyki im. Mariana Smoluchowskiegopl
dc.contributor.authorWnętrzak, Anita - 157862 pl
dc.contributor.authorŁątka, Kazimierz - 100050 pl
dc.contributor.authorDynarowicz-Łątka, Patrycja - 127845 pl
dc.date.accession2019-02-25pl
dc.date.accessioned2015-05-27T08:27:10Z
dc.date.available2015-05-27T08:27:10Z
dc.date.issued2014pl
dc.date.openaccess0
dc.description.accesstimew momencie opublikowania
dc.description.number4pl
dc.description.physical886-890pl
dc.description.versionostateczna wersja wydawcy
dc.description.volume125pl
dc.identifier.doi10.12693/APhysPolA.125.886pl
dc.identifier.eissn1898-794Xpl
dc.identifier.issn0587-4246pl
dc.identifier.projectROD UJ / Ppl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/8179
dc.identifier.weblinkhttp://przyrbwn.icm.edu.pl/APP/PDF/125/a125z4p08.pdfpl
dc.languageengpl
dc.language.containerengpl
dc.rightsUdzielam licencji. Uznanie autorstwa - Użycie niekomercyjne - Bez utworów zależnych 4.0 Międzynarodowa*
dc.rights.licenceInna otwarta licencja
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.pl*
dc.share.typeotwarte czasopismo
dc.subtypeArticlepl
dc.titleInteractions between antitumor alkylphosphocholines and membrane sphingolipids in Langmuir monolayerspl
dc.title.journalActa Physica Polonica. Apl
dc.title.volumeProceedings of the XLVIIIth Zakopane School of Physics International Symposium Breaking Frontiers : Submicron Structures in Physics and Biology, Zakopane, Poland, May 20-25, 2013 and Proceedings of the 15th International Conference on Defects Recognition, Imaging and Physics in Semiconductors Warsaw, Poland, September 15-19, 2013pl
dc.typeJournalArticlepl
dspace.entity.typePublication
cris.lastimport.wos
2024-04-09T19:01:05Z
dc.abstract.enpl
Alkylphosphocholines (APCs) are new generation, highly selective antineoplastic drugs, whose mechanism of action is not fully understood. It is known that in contrast to traditional chemotherapeutics, APCs do not induce cell death by apoptosis or necrosis as a result of DNA damage, but target cellular membranes and affect their biophysical properties. However, it is still unknown which membrane component attracts APC molecules selectively to cancer cells. In order to get insight into this issue, systematic investigations on the interactions between APCs and particular membrane components are highly required. Such experiments can be performed with the Langmuir monolayer technique, serving as a biomembrane model. Because of overexpression of gangliosides in tumor progression and the ability of APCs to insert into membrane rafts, two sphingolipids, i.e. sphingomyelin (SM) and ganglioside GM1 have been examined as potential membrane targets. In this respect, their interactions with three alkylphosphocholines, differing in their hydrophobic part: hexadecylphosphocholine (HePC), octadecylphosphocholine (OcPC) and erucylphosphocholine (ErPC) have been studied and the following systems have been analysed: SM(or GM1)/HePC, SM(or GM1)/OcPC and SM(or GM1)/ErPC. It was found that all the investigated APCs show strong affinity to ganglioside in contrast to sphingomyelin. Differences in interaction of APCs with both investigated sphingolipids were studied based on experimental surface pressure ( \pi ) versus mean molecular area (A) isotherms, and analyzed qualitatively (with mean molecular area values) as well as quantitatively (with \Delta G^{exc} function). The obtained results have also been analysed taking into consideration geometry of interacting molecules. Our results suggest that gangliosides may be molecular targets for APCs, attracting them to tumor cells. Although the interactions with sphingomyelin were found to be unfavourable, further studies on more complex system, containing APCs mixed with sphingomyelin and cholesterol, are required to better understand the role of lipid rafts in the selectivity of APCs.
dc.affiliationpl
Wydział Chemii : Zakład Chemii Ogólnej
dc.affiliationpl
Wydział Fizyki, Astronomii i Informatyki Stosowanej : Instytut Fizyki im. Mariana Smoluchowskiego
dc.contributor.authorpl
Wnętrzak, Anita - 157862
dc.contributor.authorpl
Łątka, Kazimierz - 100050
dc.contributor.authorpl
Dynarowicz-Łątka, Patrycja - 127845
dc.date.accessionpl
2019-02-25
dc.date.accessioned
2015-05-27T08:27:10Z
dc.date.available
2015-05-27T08:27:10Z
dc.date.issuedpl
2014
dc.date.openaccess
0
dc.description.accesstime
w momencie opublikowania
dc.description.numberpl
4
dc.description.physicalpl
886-890
dc.description.version
ostateczna wersja wydawcy
dc.description.volumepl
125
dc.identifier.doipl
10.12693/APhysPolA.125.886
dc.identifier.eissnpl
1898-794X
dc.identifier.issnpl
0587-4246
dc.identifier.projectpl
ROD UJ / P
dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/8179
dc.identifier.weblinkpl
http://przyrbwn.icm.edu.pl/APP/PDF/125/a125z4p08.pdf
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Udzielam licencji. Uznanie autorstwa - Użycie niekomercyjne - Bez utworów zależnych 4.0 Międzynarodowa
dc.rights.licence
Inna otwarta licencja
dc.rights.uri*
http://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.pl
dc.share.type
otwarte czasopismo
dc.subtypepl
Article
dc.titlepl
Interactions between antitumor alkylphosphocholines and membrane sphingolipids in Langmuir monolayers
dc.title.journalpl
Acta Physica Polonica. A
dc.title.volumepl
Proceedings of the XLVIIIth Zakopane School of Physics International Symposium Breaking Frontiers : Submicron Structures in Physics and Biology, Zakopane, Poland, May 20-25, 2013 and Proceedings of the 15th International Conference on Defects Recognition, Imaging and Physics in Semiconductors Warsaw, Poland, September 15-19, 2013
dc.typepl
JournalArticle
dspace.entity.type
Publication
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