Protein Coronas on Gold Nanorods Passivated with Amphiphilic Ligands Affect Cytotoxicity and Cellular Response to Penicillin/Streptomycin
Source abstract
Abstract
We probe how amphiphilic ligands (ALs) of four different types affect the formation of protein coronas on gold nanorods (NRs) and their impact on cellular response. NRs coated with cetyltrimethylammonium bromide were ligand exchanged with polyoxyethylene[10]cetyl ether, oligofectamine, and phosphatidylserine (PS). Protein coronas from equine serum (ES) were formed on these NR-ALs, and their colloidal stability, as well as cell uptake, proliferation, oxidative stress, and gene expression, were examined. We find that the protein corona that forms and its colloidal stability are affected by AL type and that the cellular response to these NR-AL-coronas (NR-AL-ES) is both ligand and corona dependent. We also find that the presence of common cell culture supplement penicillin/streptomycin can impact the colloidal stability and cellular response of NR-AL and NR-AL-ES, showing that the cell response is not necessarily inert to pen/strep when in the presence of nanoparticles. Although the protein corona is what the cells see, the underlying surface ligands evidently play an important role in shaping and defining the physical characteristics of the corona, which ultimately impacts the cellular response. Further, the results of this study suggest that the cellular behavior toward NR-AL is mediated by not only the type of AL and the protein corona it forms but also its resulting colloidal stability and interaction with cell culture supplements.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Nanoparticle-Based Drug Delivery · Polymer Surface Interaction Studies · Gold and Silver Nanoparticles Synthesis and Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Molecular Bioeffects Branch, Human Effectiveness Directorate, Air Force Research Laboratory, Wright-Patterson AFB, Dayton, Ohio 45433, United States
Funding
National Science Foundation
References (51)
Show source-provided references
1. Lundqvist M. · Proc. Natl. Acad. Sci. U.S.A. · 2008 · 105 · 1426510.1073/pnas.0805135105 ↗
2. Podila R. · Appl. Phys. Lett. · 2012 · 101 · 26370110.1063/1.4772509 ↗
3. Walkey C. D. · J. Am. Chem. Soc. · 2012 · 134 · 213910.1021/ja2084338 ↗
4. Jedlovszky-Hajdú A. · Langmuir · 2012 · 28 · 1498310.1021/la302446h ↗
5. Cukalevski R. · Langmuir · 2011 · 27 · 1436010.1021/la203290a ↗
6. Pan H. · Langmuir · 2012 · 28 · 1277910.1021/la302258k ↗
7. Tellechea E. · Langmuir · 2012 · 28 · 519010.1021/la2050866 ↗
8. Salvati A. · Nat. Nanotechnol. · 2013 · 8 · 13710.1038/nnano.2012.237 ↗
9. Mirshafiee V. · Chem. Commun. · 2013 · 49 · 255710.1039/c3cc37307j ↗
10. Dell’Orco D. · Nanomed Nanotechnol Biol. Med. · 2012 · 8 · 127110.1016/j.nano.2012.02.006 ↗
11. Hirn S. · Eur. J. Pharm. Biopharm · 2011 · 77 · 40710.1016/j.ejpb.2010.12.029 ↗
12. Deguchi S. · Chem. Res. Toxicol. · 2007 · 20 · 85410.1021/tx6003198 ↗
13. Drescher D. · Anal. Bioanal. Chem. · 2011 · 400 · 136710.1007/s00216-011-4893-7 ↗
14. Ge C. C. · Proc. Natl. Acad. Sci. U.S.A. · 2011 · 108 · 1696810.1073/pnas.1105270108 ↗
15. Bajaj A. · J. Mater. Chem. · 2009 · 19 · 632810.1039/b901616c ↗
16. Maiorano G. · ACS Nano · 2010 · 4 · 748110.1021/nn101557e ↗
17. Wang G. K. · Nanomed Nanotechnol Biol. Med. · 2012 · 8 · 82210.1016/j.nano.2011.10.007 ↗
18. Grabinski C. · ACS Nano · 2011 · 5 · 287010.1021/nn103476x ↗
19. Oh W. K. · ACS Nano · 2010 · 4 · 530110.1021/nn100561e ↗
20. Mortensen N. P. · Nanoscale · 2013 · 5 · 637210.1039/c3nr33280b ↗
21. Alkilany A. M. · Small · 2012 · 8 · 127010.1002/smll.201101948 ↗
22. Lee S. E. · ACS Nano · 2012 · 6 · 777010.1021/nn301744x ↗
23. Lee S. E. · J. Am. Chem. Soc. · 2009 · 131 · 1406610.1021/ja904326j ↗
24. Li P. C. · Biomaterials · 2008 · 29 · 361710.1016/j.biomaterials.2008.05.020 ↗
25. Orendorff C. J. · ACS Nano · 2009 · 3 · 97110.1021/nn900037k ↗
26. Takahashi H. · Langmuir · 2006 · 22 · 210.1021/la0520029 ↗
27. Ba H. J. · Nano Lett. · 2010 · 10 · 300610.1021/nl101454a ↗
28. Alkilany A. M. · Small · 2009 · 5 · 70110.1002/smll.200801546 ↗
29. Wang L. · Nanoscale · 2013 · 5 · 838410.1039/c3nr01626a ↗
30. Chen C.-C. · J. Am. Chem. Soc. · 2006 · 128 · 370910.1021/ja0570180 ↗
31. Cobley C. M. · Chem. Soc. Rev. · 2011 · 40 · 4410.1039/B821763G ↗
32. Kah J. C. · ACS Nano · 2012 · 6 · 673010.1021/nn301389c ↗
33. Cifuentes-Rius A. · ACS Nano · 2013 · 7 · 1006610.1021/nn404166q ↗
34. Hühn D. · ACS Nano · 2013 · 7 · 325310.1021/nn3059295 ↗
35. Kah J. C. Y. · Langmuir · 2012 · 28 · 883410.1021/la3000944 ↗
36. Dominguez-Medina S. · ACS Sustainable Chem. Eng. · 2013 · 1 · 83310.1021/sc400042h ↗
37. Gebauer J. S. · Langmuir · 2012 · 28 · 967310.1021/la301104a ↗
38. Audouy S. · J. Gene Med. · 2000 · 2 · 46510.1002/1521-2254(200011/12)2:6<465::AID-JGM141>3.0.CO;2-Z ↗
39. Verma A. · Small · 2010 · 6 · 1210.1002/smll.200901158 ↗
40. Rauch J. · Chem. Rev. · 2013 · 113 · 339110.1021/cr3002627 ↗
41. Sahay G. · J. Controlled Release · 2010 · 145 · 18210.1016/j.jconrel.2010.01.036 ↗
42. Hinderliter P. M. · Part Fibre Toxicol. · 2010 · 7 · 3610.1186/1743-8977-7-36 ↗
43. Cho E. C. · Nat. Nanotechnol. · 2011 · 6 · 38510.1038/nnano.2011.58 ↗
44. Epstein J. · In Vitro Cell. Dev. Biol. · 1990 · 26 · 112110.1007/BF02623686 ↗
45. Hu W. · ACS Nano · 2011 · 5 · 369310.1021/nn200021j ↗
46. Hawley-Nelson P. · 2008 · 9.4.1
47. Schaeublin N. M. · Nanoscale · 2011 · 3 · 41010.1039/c0nr00478b ↗
48. Czekay R. P. · Int. J. Cell Biol. · 2011 · 2011 · 56248110.1155/2011/562481 ↗
49. Aggarwal B. B. · Nat. Rev. Immunol · 2003 · 3 · 74510.1038/nri1184 ↗
50. Alberts B. · 2008
51. Sau T. K. · Langmuir · 2004 · 20 · 641410.1021/la049463z ↗