Lipid Vesicle Interaction with Hydrophobic Surfaces: A Coarse-Grained Molecular Dynamics Study
Source abstract
Abstract
Active surfaces are presently tailored to cause specific effects on living cells, which can be useful in many fields. Their development requires the understanding of the molecular mechanisms of interaction between lipid-enveloped entities and solid surfaces. Here, using coarse-grained molecular dynamics simulations, we have analyzed the different interaction modes of coated substrates with lipid vesicles that mimic biological envelopes. For neutral and hydrophobically functionalized substrates, three action modes on contacting vesicles have been obtained including intact, partially broken, and completely destroyed vesicles. The molecular mechanisms for each interaction pathway and the corresponding energy balances have been analyzed in detail. Interestingly, we have shown that any specific action mode can be obtained by appropriately tailoring the wetting characteristics of the surface coating. In particular, we have shown that surfaces that are simultaneously hydrophobic and oleophilic are optimal to fully disrupt the contacting vesicle lipid bilayer.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Lipid Membrane Structure and Behavior · Surfactants and Colloidal Systems · Supramolecular Self-Assembly in Materials
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
ICFO-Institut de Ciències Fotòniques, The Barcelona Institute of Science and Technology, Castelldefels Barcelona 08860, Spain
ICREA-Institució Catalana de Recerca i Estudis Avançats, Passeig Lluís Companys, 23, 08010 Barcelona, Spain
Funding
Fundación Cellex · Ministerio de Economía y Competitividad · Agència de Gestió d'Ajuts Universitaris i de Recerca · European Regional Development Fund
References (28)
Show source-provided references
1. Ratner B. D. · 2004
2. 10.1016/j.porgcoat.2003.06.00110.1016/j.porgcoat.2003.06.001 ↗
3. 10.1021/es061537110.1021/es0615371 ↗
4. 10.1016/0304-4157(86)90016-X10.1016/0304-4157(86)90016-X ↗
5. Tampé R. · 1996
6. 10.1038/1509010.1038/15090 ↗
7. 10.1021/la800211v10.1021/la800211v ↗
8. 10.1038/nnano.2013.12510.1038/nnano.2013.125 ↗
9. 10.1073/pnas.060880310310.1073/pnas.0608803103 ↗
10. 10.1073/pnas.101701210810.1073/pnas.1017012108 ↗
11. 10.1021/acsami.6b0277910.1021/acsami.6b02779 ↗
12. 10.1021/jp077305l10.1021/jp077305l ↗
13. 10.1063/1.300806010.1063/1.3008060 ↗
14. Hoopes M. I. · 2009 · 10110.1007/978-1-60761-314-5_4 ↗
15. 10.1016/j.chemphyslip.2009.03.00310.1016/j.chemphyslip.2009.03.003 ↗
16. 10.2174/15734131179748368210.2174/157341311797483682 ↗
17. 10.1039/C2SM27450G10.1039/C2SM27450G ↗
18. 10.1021/la400119e10.1021/la400119e ↗
19. 10.1021/acs.langmuir.6b0004310.1021/acs.langmuir.6b00043 ↗
20. 10.1021/jp071097f10.1021/jp071097f ↗
21. 10.1039/c3cs60093a10.1039/c3cs60093a ↗
22. 10.1073/pnas.091516910710.1073/pnas.0915169107 ↗
23. 10.1039/C4CP03519D10.1039/C4CP03519D ↗
24. 10.1021/ja983582h10.1021/ja983582h ↗
25. 10.1021/ja00074a00410.1021/ja00074a004 ↗
26. 10.1007/s00894010004510.1007/s008940100045 ↗
27. 10.1016/j.fluid.2012.07.01010.1016/j.fluid.2012.07.010 ↗
28. 10.1021/acs.est.5b0464410.1021/acs.est.5b04644 ↗