journal article·2012-08-21

Nonionic Block Copolymers Assemble on the Surface of Protein Bionanoparticle

Zhi Liu, Jingxia Gu, Man Wu, Shidong Jiang, Dayong Wu, Qian Wang, Zhongwei Niu, Yong Huang

Langmuir· Volume 28· Issue 33
Publisher page

Abstract

Efficient delivery of therapeutic proteins to a target site remains a challenge due to rapid clearance from the body. Here, we selected tobacco mosaic virus (TMV) as a model protein system to investigate the interactions between the protein and a nonionic block copolymer as a possible protecting agent for the protein. By varying the temperature, we were able to obtain core-shell structures based on hydrophobic interactions among PO blocks and noncovalent interactions between TMV and EO blocks. The protein-polymer interactions were characterized by dynamic light scattering and isothermal titration calorimetry. This study establishes principles for the possible design of clinically useful protein delivery systems.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Protein purification and stability · Bacteriophages and microbial interactions · Viral Infectious Diseases and Gene Expression in Insects

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

Affiliations

National Research Centre of Engineering Plastics, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100084, China

Department of Chemistry and Biochemistry and Nanocenter, University of South Carolina, 631 Sumter Street, Columbia, South Carolina 29208, United States

References (27)

Show source-provided references
1. Pavlou A. K. · Nat. Biotechnol. · 2004 · 22 · 151310.1038/nbt1204-1513 ↗
2. Harris J. M. · Nat. Rev. Drug Discovery · 2003 · 2 · 21410.1038/nrd1033 ↗
3. Roberts M. J. · Adv. Drug Delivery Rev. · 2002 · 54 · 45910.1016/S0169-409X(02)00022-4 ↗
4. Chapman A. P. · Adv. Drug Delivery Rev. · 2002 · 54 · 53110.1016/S0169-409X(02)00026-1 ↗
5. Veronese F. M. · Biomaterials · 2001 · 22 · 40510.1016/S0142-9612(00)00193-9 ↗
6. Wiradharma N. · Nano Today · 2009 · 4 · 30210.1016/j.nantod.2009.06.001 ↗
7. Tanner P. · Acc. Chem. Res. · 2011 · 44 · 103910.1021/ar200036k ↗
8. Lee Y. · J. Am. Chem. Soc. · 2007 · 129 · 536210.1021/ja071090b ↗
9. Blanazs A. · Macromol. Rapid Commun. · 2009 · 30 · 26710.1002/marc.200800713 ↗
10. Soto C. M. · Curr. Opin. Biotechnol. · 2010 · 21 · 42610.1016/j.copbio.2010.07.004 ↗
11. Kabanov A. V. · J. Controlled Release · 2002 · 82 · 18910.1016/S0168-3659(02)00009-3 ↗
12. Kabanov A. V. · Adv. Drug Delivery Rev. · 2002 · 54 · 75910.1016/S0169-409X(02)00047-9 ↗
13. Chen G. · Chem. Soc. Rev. · 2011 · 40 · 225410.1039/c0cs00153h ↗
14. Harada A. · Chem. Rev. · 2009 · 109 · 597410.1021/cr9000622 ↗
15. Li J. · Macromolecules · 2001 · 34 · 723610.1021/ma010742s ↗
16. Fujita H. · Macromolecules · 1999 · 32 · 253410.1021/ma9814550 ↗
17. Joseph J. · Langmuir · 2007 · 23 · 46010.1021/la061850g ↗
18. Dreiss C. A. · Soft Matter · 2009 · 5 · 188810.1039/b812805g ↗
19. Jansson J. · J. Phys. Chem. B · 2004 · 108 · 8210.1021/jp030792u ↗
20. Alexandridis P. · Langmuir · 1995 · 11 · 146810.1021/la00005a011 ↗
21. Guo C. · Langmuir · 1999 · 15 · 270310.1021/la981036w ↗
22. Liang X. F. · J. Phys. Chem. B · 2007 · 111 · 1321710.1021/jp074990n ↗
23. Li M. · J. Am. Chem. Soc. · 2010 · 132 · 1705210.1021/ja109084h ↗
24. De M. · J. Am. Chem. Soc. · 2007 · 129 · 1074710.1021/ja071642q ↗
25. Zeng H. Q. · J. Am. Chem. Soc. · 2002 · 124 · 290310.1021/ja010701b ↗
26. Jorgensen E. B. · Macromolecules · 1997 · 30 · 235510.1021/ma9616322 ↗
27. Bahadur P. · Colloid Polym. Sci. · 1993 · 271 · 65710.1007/BF00652828 ↗