journal article·2013-12

A Simple and Versatile Method for the Formation of Arrays of Giant Vesicles with Controlled Size and Composition

You Jung Kang, Harrison S. Wostein, Sheereen Majd

Advanced Materials· Volume 25· Issue 47
Publisher page

Abstract

A simple and versatile method for the Formation of Arrays of Giant Vesicles with Controlled Size and Composition. The ability of this technique to generate arrays of giant liposomes from a wide range of membrane lipids and protein compositions is demonstrated. The resulting vesicles are utilized for studying protein activity, lipid-protein interactions, and protein-protein interactions. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Lipid Membrane Structure and Behavior · RNA Interference and Gene Delivery · Nanopore and Nanochannel Transport Studies

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Bioengineering The Pennsylvania State University Hallowell Building University Park PA 16802 USA

Department of Bioengineering Department of Engineering Science and Mechanics Materials Research Institute The Pennsylvania State University Hallowell Building University Park PA 16802 USA

References (38)

Show source-provided references
1. 10.1016/S0006-3495(03)74726-210.1016/S0006-3495(03)74726-2 ↗
2. 10.1016/S0006-3495(00)76592-110.1016/S0006-3495(00)76592-1 ↗
3. 10.1039/b713982a10.1039/b713982a ↗
4. 10.1007/s00232-010-9227-810.1007/s00232-010-9227-8 ↗
5. 10.1021/ac034020610.1021/ac0340206 ↗
6. 10.1021/ac048207o10.1021/ac048207o ↗
7. 10.1002/smll.20090056010.1002/smll.200900560 ↗
8. 10.1080/1040923090307454910.1080/10409230903074549 ↗
9. 10.1002/anie.20035186610.1002/anie.200351866 ↗
10. Osaki T. · IEEE 24th Int. Conf. MEMS · 2011
11. 10.1021/ja02978310.1021/ja029783 ↗
12. 10.3390/s10121135210.3390/s101211352 ↗
13. 10.1038/nchembio.21310.1038/nchembio.213 ↗
14. 10.1073/pnas.070611410410.1073/pnas.0706114104 ↗
15. 10.1073/pnas.060603210310.1073/pnas.0606032103 ↗
16. 10.1021/ja049023u10.1021/ja049023u ↗
17. 10.1007/BFb011629510.1007/BFb0116295 ↗
18. 10.1016/j.chemphyslip.2008.03.00810.1016/j.chemphyslip.2008.03.008 ↗
19. 10.1039/b308082j10.1039/b308082j ↗
20. 10.1016/j.colsurfb.2005.01.01610.1016/j.colsurfb.2005.01.016 ↗
21. 10.1021/la001757710.1021/la0017577 ↗
22. 10.1002/smll.20110209610.1002/smll.201102096 ↗
23. 10.1002/anie.20050218910.1002/anie.200502189 ↗
24. 10.1002/smll.20060043110.1002/smll.200600431 ↗
25. 10.1016/j.surfrep.2006.06.00110.1016/j.surfrep.2006.06.001 ↗
26. 10.1002/adma.20080186410.1002/adma.200801864 ↗
27. Majd S. · Calcium Binding Proteins · 2006 · 1 · 4
28. 10.1002/pmic.20030074810.1002/pmic.200300748 ↗
29. 10.1021/la971331110.1021/la9713311 ↗
30. 10.1021/ja805548510.1021/ja8055485 ↗
31. 10.1016/j.biomaterials.2005.05.00110.1016/j.biomaterials.2005.05.001 ↗
32. 10.1021/la047173c10.1021/la047173c ↗
33. 10.1073/pnas.070876210410.1073/pnas.0708762104 ↗
34. 10.1006/jmbi.1999.303210.1006/jmbi.1999.3032 ↗
35. 10.1074/jbc.M00364920010.1074/jbc.M003649200 ↗
36. 10.1016/0003-9861(92)90111-910.1016/0003-9861(92)90111-9 ↗
37. 10.1021/ja304721r10.1021/ja304721r ↗
38. 10.1038/nmat244610.1038/nmat2446 ↗