journal article·2013-05-22Open access

Stable Conjugates of Peptides with Gold Nanorods for Biomedical Applications with Reduced Effects on Cell Viability

Carolina Adura, Simon Guerrero, Edison Salas, Luis Medel, Ana Riveros, Juan Mena, Jordi Arbiol, Fernando Albericio, Ernest Giralt, Marcelo J. Kogan

Abstract

Gold nanorods used in therapy and diagnosis must be nontoxic and stable in biological media and should be specific for the target. The complete combination of these three factors has hindered the use of gold nanorods as carriers in biological and biomedical applications. In this study, we produced a conjugate of gold nanorods with the peptide CLPFFD that recognizes toxic β-amyloid aggregates present in Alzheimer's disease, demonstrates colloidal stability, maintains plasmonic properties, and shows no effects on cell viability in the SH-SY5Y cell line. Furthermore, the irradiation of β-amyloid in the presence of the conjugate with near-infrared region irradiation energy reduces the amyloidogenic process reducing also its cytotoxicity. The nanorods were synthesized following the seed-mediated method in cetyltrimethylammonium bromide (CTAB) and were conjugated with the N-terminal cysteine peptide, CLPFFD. The conjugate was exhaustively characterized using different techniques (Absorption spectroscopy, X-ray photoelectron spectroscopy, electron energy loss spectroscopy, and zeta potential). The effects on cell viability and cell penetration by transmission electron microscopy of the conjugate were evaluated. The chemisorption of the peptide on the surface of gold nanorods increases their stability and reduces their effects on cell viability.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Gold and Silver Nanoparticles Synthesis and Applications · Nanocluster Synthesis and Applications · Quantum Dots Synthesis And Properties

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

Affiliations

Facultad de Química y Biología, Universidad de Santiago de Chile, Santiago, Chile

Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile

Institut de Ciència de Materials de Barcelona, ICMAB-CSIC, Bellaterra, 08193, CAT, Spain

Institució Catalana de Recerca i Estudis Avançats (ICREA), 08010 Barcelona, CAT, Spain

Institute for Research in Biomedicine, IRB Barcelona, 08028-Barcelona, Spain

Department of Organic Chemistry, University of Barcelona, 08028-Barcelona, Spain

CIBER-BBN Networking Centre on Bioengineering, Biomaterials, and Nanomedicine, Barcelona Science Park, 08028-Barcelona, Spain

School of Chemistry and Physics, University of KwaZulu-Natal, 4001-Durban, South Africa

References (60)

Show source-provided references
1. Marcon L. · Bioconjugate Chem. · 2008 · 19 · 80210.1021/bc8000084 ↗
2. Katz E. · Angew. Chem., Int. Ed. · 2004 · 43 · 604210.1002/anie.200400651 ↗
3. Kogan M. J. · Nanomedicine · 2007 · 2 · 28710.2217/17435889.2.3.287 ↗
4. Kim J. · Angew. Chem., Int. Ed. · 2006 · 45 · 775410.1002/anie.200602471 ↗
5. Panyam J. · FASEB J. · 2002 · 16 · 121710.1096/fj.02-0088com ↗
6. Kogan M. J. · Nano Lett. · 2006 · 6 · 11010.1021/nl0516862 ↗
7. El-Sayed I. H. · Nano Lett. · 2005 · 5 · 82910.1021/nl050074e ↗
8. Yguerabide J. · J. Cell Biochem. · 2001 · 84 · 7110.1002/jcb.10077 ↗
9. Karhanek M. · Nano Lett. · 2005 · 5 · 40310.1021/nl0480464 ↗
10. Taton T. A. · J. Am. Chem. Soc. · 2001 · 123 · 516410.1021/ja0102639 ↗
11. Kohler N. · Langmuir · 2005 · 21 · 885810.1021/la0503451 ↗
12. Yang P. H. · Bioconjugate Chem. · 2005 · 16 · 49410.1021/bc049775d ↗
13. Hirsch L. R. · Proc. Natl. Acad. Sci. U.S.A. · 2003 · 100 · 1354910.1073/pnas.2232479100 ↗
14. Kogan M. J. · Nanoscale Res. Lett. · 2008 · 3 · 43510.1007/s11671-008-9178-5 ↗
15. Huo Q. · Colloids Surf., B · 2008 · 63 · 20010.1016/j.colsurfb.2007.12.006 ↗
16. Barnes D. E. · Lancet Neurol. · 2011 · 10 · 81910.1016/S1474-4422(11)70072-2 ↗
17. Mullerhill B. · Annu. Rev. Biochem. · 1989 · 58 · 28710.1146/annurev.bi.58.070189.001443 ↗
18. Crouch P. J. · Int. J. Biochem. Cell B · 2008 · 40 · 18110.1016/j.biocel.2007.07.013 ↗
19. Estrada L. D. · Curr. Top. Med. Chem. · 2007 · 7 · 11510.2174/156802607779318262 ↗
20. El-Sayed M. A. · Adv. Mater. · 2009 · 21 · 488010.1002/adma.200802789 ↗
21. Weissleder R. · Nat. Biotechnol. · 2001 · 19 · 31610.1038/86684 ↗
22. Nikoobakht B. · Chem. Mater. · 2003 · 15 · 195710.1021/cm020732l ↗
23. Broderick G. · J. Dairy Sci. · 1989 · 72 · 254010.3168/jds.S0022-0302(89)79394-2 ↗
24. Cortesi R. · Int. J. Pharm. · 1996 · 139 · 6910.1016/0378-5173(96)04574-7 ↗
25. van Ruissen F. · J. Invest. Dermatol. · 1998 · 110 · 35810.1046/j.1523-1747.1998.00155.x ↗
26. Huff T. B. · Langmuir · 2007 · 23 · 159610.1021/la062642r ↗
27. Niidome Y. · Chem. Commun. · 2007 · 377710.1039/b706671f ↗
28. Takahashi H. · J. Nanopart. Res. · 2008 · 10 · 22110.1007/s11051-007-9227-5 ↗
29. Connor E. E. · Small · 2005 · 1 · 32510.1002/smll.200400093 ↗
30. Lee S. E. · J. Am. Chem. Soc. · 2009 · 131 · 1406610.1021/ja904326j ↗
31. Didychuk C. L. · Proc. SPIE · 2008 · 6856 · 68560M110.1117/12.791307 ↗
32. Orendorff C. J. · ACS Nano · 2009 · 3 · 97110.1021/nn900037k ↗
33. MacQueen A. · The 2007 NNIN REU Research Accomplishments · 2007 · 32
34. Link S. · J. Chem. Phys. · 2001 · 114 · 236210.1063/1.1336140 ↗
35. Bieschke J. · Biochemistry · 2008 · 47 · 5010.1021/bi701757v ↗
36. Goy-Lopez S. · Langmuir · 2012 · 28 · 911310.1021/la300402w ↗
37. Zhuohua Z. · Nature · 1998 · 395 · 69810.1038/27208 ↗
38. Soto C. · Nat. Med. · 1998 · 4 · 82210.1038/nm0798-822 ↗
39. Tielens F. · J. Phys. Chem. C · 2010 · 114 · 944410.1021/jp102036r ↗
40. Jana N. R. · Chem. Mater. · 2001 · 13 · 231310.1021/cm000662n ↗
41. Grzelczak M. · Chem. Soc. Rev. · 2008 · 37 · 178310.1039/b711490g ↗
42. Tiwari N. · Plasmonics · 2007 · 2 · 23110.1007/s11468-007-9043-x ↗
43. Olmedo I. · Bioconjugate Chem. · 2008 · 19 · 115410.1021/bc800016y ↗
44. Sethi M. · Langmuir · 2010 · 26 · 1512110.1021/la100034q ↗
45. Caswell K. K. · J. Am. Chem. Soc. · 2003 · 125 · 1391410.1021/ja037969i ↗
46. Gunawan C. · Small · 2009 · 5 · 34110.1002/smll.200801202 ↗
47. Vericat C. · J. Phys.: Condens. Matter · 2008 · 20 · 184004
48. Lau K. H. A. · Langmuir · 2006 · 22 · 296810.1021/la053248g ↗
49. Jiang P. · J. Phys. D: Appl. Phys. · 2001 · 34 · 225510.1088/0022-3727/34/15/303 ↗
50. Brust M. · J. Chem. Soc., Chem. Commun. · 1994 · 80110.1039/C39940000801 ↗
51. Hubert F. · Langmuir · 2008 · 24 · 921910.1021/la801711q ↗
52. Funston A. M. · Nano Lett. · 2009 · 9 · 165110.1021/nl900034v ↗
53. Levine H. · Protein Sci. · 1993 · 2 · 40410.1002/pro.5560020312 ↗
54. Dobrovolskaia M. A. · Nanomed. Nanotechnol. · 2009 · 5 · 10610.1016/j.nano.2008.08.001 ↗
55. Alkilany A. M. · Langmuir · 2010 · 26 · 932810.1021/la100253k ↗
56. Wang L. M. · Nano Lett. · 2011 · 11 · 77210.1021/nl103992v ↗
57. Pujals S. · Biochim. Biophys. Acta, Biomembr. · 2006 · 1758 · 26410.1016/j.bbamem.2006.01.006 ↗
58. Chanda N. · Nano Lett. · 2009 · 9 · 179810.1021/nl8037147 ↗
59. Yaar M. · Neuropathol. Appl. Neurobiol. · 2007 · 33 · 53310.1111/j.1365-2990.2007.00844.x ↗
60. Xue D. · Neurobiol. Dis. · 2012 · 46 · 70110.1016/j.nbd.2012.03.013 ↗