journal article·2019-12-18

Giant “Breathing” Proteinosomes with Jellyfish-like Property

Tingting Wang, Jiayun Xu, Xiaotong Fan, Xu Yan, Dong Yao, Ruyu Li, Shengda Liu, Xiumei Li, Junqiu Liu

ACS Applied Materials & Interfaces· Volume 11· Issue 50
Publisher page

Abstract

The design and construction of "breathing" self-assemblies has been a rather popular topic due to their potential in materials science and nanotechnology. Inspired by the "breathing" behavior of natural jellyfish, herein, we presented the construction of a giant "breathing" proteinosome through an interfacial self-assembly of proteins and surfactants at the oil/water interface of emulsions: The proteinosome displays "breathing" behavior and can swell and shrink for multiple cycles by protein folding and unfolding through the alternate addition and removal of denaturant; more importantly, when green fluorescent proteins were selected as alternative protein building blocks, the fluorescence of proteinosome can be reversibly switched on/off just like the behavior of jellyfish. Moreover, accompanied by reversible swelling and shrinking and on/off fluorescence, the expanded and shrunk membrane pore can be tuned for distinguishing quantum dots of different sizes. The folding-responsive breathing behavior of intelligent proteinosomes provides a platform for functional biomaterials.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Lipid Membrane Structure and Behavior · Photoreceptor and optogenetics research · Hemoglobin structure and function

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

Affiliations

State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun 130012, China

Funding

Ministry of Science and Technology of the People's Republic of China · National Natural Science Foundation of China

References (39)

Show source-provided references
1. 10.1021/ar700191410.1021/ar7001914 ↗
2. 10.1021/cr200157d10.1021/cr200157d ↗
3. 10.1002/anie.20120104010.1002/anie.201201040 ↗
4. 10.1126/science.123180610.1126/science.1231806 ↗
5. 10.1021/ja902869q10.1021/ja902869q ↗
6. 10.1002/anie.20130039710.1002/anie.201300397 ↗
7. 10.1126/science.107497210.1126/science.1074972 ↗
8. 10.1002/anie.20070320310.1002/anie.200703203 ↗
9. 10.1002/anie.20130398410.1002/anie.201303984 ↗
10. 10.1039/C5CS00199D10.1039/C5CS00199D ↗
11. 10.1021/ja809475a10.1021/ja809475a ↗
12. 10.1002/ange.20090107110.1002/ange.200901071 ↗
13. Angew. Chem., Int. Ed. · 2009 · 48 · 565310.1002/anie.200901071 ↗
14. 10.1021/ja908124g10.1021/ja908124g ↗
15. 10.1016/j.addr.2012.02.00610.1016/j.addr.2012.02.006 ↗
16. 10.1039/c2cs35103j10.1039/c2cs35103j ↗
17. 10.1039/C4CC06629D10.1039/C4CC06629D ↗
18. 10.1002/anie.20120636210.1002/anie.201206362 ↗
19. 10.1002/anie.20110070810.1002/anie.201100708 ↗
20. 10.1002/anie.20100144210.1002/anie.201001442 ↗
21. 10.1038/ncomms323910.1038/ncomms3239 ↗
22. 10.1039/C4CC02256D10.1039/C4CC02256D ↗
23. 10.1021/la304298810.1021/la3042988 ↗
24. 10.1021/acsami.7b0818610.1021/acsami.7b08186 ↗
25. 10.1002/anie.20140810510.1002/anie.201408105 ↗
26. 10.1021/jacs.6b1137110.1021/jacs.6b11371 ↗
27. 10.1039/C8NR10070E10.1039/C8NR10070E ↗
28. 10.1039/c2cs15329g10.1039/c2cs15329g ↗
29. 10.1002/smll.20190035010.1002/smll.201900350 ↗
30. 10.1039/B815884C10.1039/B815884C ↗
31. 10.1002/anie.20080476310.1002/anie.200804763 ↗
32. 10.1039/c0cc03971c10.1039/c0cc03971c ↗
33. 10.1002/anie.20110881410.1002/anie.201108814 ↗
34. 10.1021/ed082p8510.1021/ed082p85 ↗
35. 10.1038/358302a010.1038/358302a0 ↗
36. 10.1126/science.107837610.1126/science.1078376 ↗
37. 10.1038/4226410.1038/42264 ↗
38. 10.1039/C4CC04000G10.1039/C4CC04000G ↗
39. 10.1039/C7PY00963A10.1039/C7PY00963A ↗