journal article·2020

Co-assembly of HPV capsid proteins and aggregation-induced emission fluorogens for improved cell imaging

Jiangbo Jing, Ya-Rong Xue, Yu-Xue Liu, Bin Xu, Hong-Wei Li, Leijing Liu, Yuqing Wu, Wenjing Tian

Nanoscale· Volume 12· Issue 9
Publisher page

Abstract

In order to improve the cell-imaging ability, and particularly, to extend the bio-application of AIEgen, human papillomavirus (HPV) capsid protein L1 was assembled with the complex of DNA and aggregation-induced emission fluorogen 9,10-distyrylhydrazine (DSAI), where the virus-like particles (VLPs) of HPV encapsulate the complex via electrostatic interaction. The co-assembled nanoparticles, DSAI-DNA@VLPs, showed homogeneous size (∼53 nm), enhanced fluorescence (8 × 2.5-fold), considerable stability (anti-DNase digestion), improved biocompatibility and commendable protection for the DSAI-DNA complex, ensuring virtual brighter imaging in live cells, both for HeLa and normal 293T cell lines.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Luminescence and Fluorescent Materials · Nanoplatforms for cancer theranostics · Supramolecular Self-Assembly in Materials

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

Affiliations

State Key Laboratory of Supramolecular Structure and Materials

Jilin University

Changchun 130012

China

Funding

National Natural Science Foundation of China · Jilin University

References (30)

Show source-provided references
1. Zhu · J. Am. Chem. Soc. · 2007 · 129 · 352410.1021/ja068452k ↗
2. Zhang · Nanoscale · 2012 · 4 · 558110.1039/c2nr31281f ↗
3. Wang · Biomaterials · 2011 · 32 · 111010.1016/j.biomaterials.2010.09.069 ↗
4. Li · Adv. Mater. · 2008 · 20 · 476510.1002/adma.200801056 ↗
5. Murphy · Acc. Chem. Res. · 2008 · 41 · 172110.1021/ar800035u ↗
6. Li · Chem. Soc. Rev. · 2014 · 43 · 657010.1039/C4CS00014E ↗
7. Zhang · Polym. Chem. · 2014 · 5 · 39910.1039/C3PY00984J ↗
8. Fan · Nat. Nanotechnol. · 2016 · 11 · 38810.1038/nnano.2015.312 ↗
9. Yuan · Adv. Mater. · 2010 · 22 · 215910.1002/adma.200904056 ↗
10. Hong · Chem. Soc. Rev. · 2011 · 40 · 536110.1039/c1cs15113d ↗
11. Luo · Chem. Commun. · 2001 · 174010.1039/b105159h ↗
12. Wilhelm · Nat. Rev. Mater. · 2016 · 1 · 1
13. Li · Adv. Funct. Mater. · 2012 · 22 · 310710.1002/adfm.201102234 ↗
14. Rossmann · Nature · 1985 · 317 · 14510.1038/317145a0 ↗
15. Ros · Viruses · 2017 · 9 · 31310.3390/v9110313 ↗
16. Douglas · Science · 2006 · 312 · 87310.1126/science.1123223 ↗
17. Aniagyei · J. Mater. Chem. · 2008 · 18 · 376310.1039/b805874c ↗
18. Kirnbauer · J. Virol. · 1993 · 67 · 692910.1128/JVI.67.12.6929-6936.1993 ↗
19. Cerqueira · Virus Res. · 2017 · 231 · 10310.1016/j.virusres.2016.11.010 ↗
20. Huang · Biosens. Bioelectron. · 2015 · 68 · 44210.1016/j.bios.2015.01.039 ↗
21. Wang · Protein Expression Purif. · 2017 · 133 · 11010.1016/j.pep.2017.03.003 ↗
22. Jia · ACS Appl. Mater. Interfaces · 2018 · 10 · 3574510.1021/acsami.8b11556 ↗
23. Kuppeveld · FEMS Immunol. Med. Microbiol. · 2002 · 34 · 20110.1111/j.1574-695X.2002.tb00625.x ↗
24. Chen · Mol. Cell · 2000 · 5 · 55710.1016/S1097-2765(00)80449-9 ↗
25. Zdanowicz · Acta Biochim. Pol. · 2016 · 63 · 46910.18388/abp.2016_1275 ↗
26. Bishop · J. Biol. Chem. · 2007 · 282 · 3180310.1074/jbc.M706380200 ↗
27. Zheng · Chem. Commun. · 2013 · 49 · 854610.1039/c3cc44986f ↗
28. Ma · Anal. Methods · 2014 · 6 · 233810.1039/C3AY42255K ↗
29. Fu · ACS Appl. Mater. Interfaces · 2018 · 10 · 613710.1021/acsami.7b17082 ↗
30. Williams · J. Biol. Chem. · 1981 · 256 · 757310.1016/S0021-9258(19)69000-9 ↗