Journals / Turkish Journal of Chemistry / 2015 / Cilt: 39 - Sayı: 4

Functional gold nanoparticle coated surfaces for CA 125 cancer biomarker detection

Pages
697–713
Publication Date
2015-08-13
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Large spectral red shifts are very promising in terms of using these surfaces as LSPR biosensors.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Here we describe the detailed characterization of gold nanoparticle (Au Np) functionalized surfaces as a biosensing platform by studying a model streptavidin (SA)-biotin interaction.
📊
Key Findings & Data:The immobilization method and atomic concentrations of Si 2p, Au 4f, S 2p, C 1s, N 1s, and O 1s of the resulting SA-biotin modified Si surface were determined by XPS.
💡
Conclusion & Impact:Large spectral red shifts are very promising in terms of using these surfaces as LSPR biosensors.
🔬Design:Modeling & Simulation
📍Scope:Comprehensive Sample
⚙️Variables:Au Np · bioconjugation · streptavidin

Abstract

Here we describe the detailed characterization of gold nanoparticle (Au Np) functionalized surfaces as a biosensing platform by studying a model streptavidin (SA)-biotin interaction. Conjugation of SA on Au Np immobilized on silicon (Si) and quartz surfaces and its interaction with biotin were characterized by X-ray photoelectron spectroscopy (XPS), UV-Vis spectroscopy, circular dichromism (CD) spectroscopy, and contact angle measurements. The immobilization method and atomic concentrations of Si 2p, Au 4f, S 2p, C 1s, N 1s, and O 1s of the resulting SA-biotin modified Si surface were determined by XPS. The CD spectrum and confocal microscopy imaging confirmed that step-by-step modification and bioconjugation can be monitored successfully. Such detailed and well-defined step-by-step characterization provides good information about the surface properties of biosensor platforms. In addition, the LSPR sensing ability of the Au Np based platforms was studied by using a model SA-biotin system. A 20 nm spectral red shift was detected when 150 nM SA was immobilized on to the Au Nps surface using the direct incubation/binding method on to the dry surface instead of the flow-injection method. The same platforms were also used to detect the CA 125 antibody-antigen system. Large spectral red shifts are very promising in terms of using these surfaces as LSPR biosensors.

Özet

Here we describe the detailed characterization of gold nanoparticle (Au Np) functionalized surfaces as a biosensing platform by studying a model streptavidin (SA)-biotin interaction. Conjugation of SA on Au Np immobilized on silicon (Si) and quartz surfaces and its interaction with biotin were characterized by X-ray photoelectron spectroscopy (XPS), UV-Vis spectroscopy, circular dichromism (CD) spectroscopy, and contact angle measurements. The immobilization method and atomic concentrations of Si 2p, Au 4f, S 2p, C 1s, N 1s, and O 1s of the resulting SA-biotin modified Si surface were determined by XPS. The CD spectrum and confocal microscopy imaging confirmed that step-by-step modification and bioconjugation can be monitored successfully. Such detailed and well-defined step-by-step characterization provides good information about the surface properties of biosensor platforms. In addition, the LSPR sensing ability of the Au Np based platforms was studied by using a model SA-biotin system. A 20 nm spectral red shift was detected when 150 nM SA was immobilized on to the Au Nps surface using the direct incubation/binding method on to the dry surface instead of the flow-injection method. The same platforms were also used to detect the CA 125 antibody-antigen system. Large spectral red shifts are very promising in terms of using these surfaces as LSPR biosensors.

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Cite This Article

TUNÇ, İ., SUSAPTO, H. H., GÜLER, M. Ö. (2015). Functional gold nanoparticle coated surfaces for CA 125 cancer biomarker detection. Turkish Journal of Chemistry, Cilt: 39 - Sayı: 4, 697–713. https://ajindex.com/articles/185211

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References (25)

  1. Luppa, P. B.; Sokoll, L. J.; Chan, D. W. Clin. Chim. Acta 2001, 314, 1–26
  2. Boujday, S.; Bantegnie, A.; Briand, E.; Marnet, P. G.; Salmain, M.; Pradier, C. M. J. Phys. Chem. B 2008, 112, 6708–6715
  3. Hutter, E.; Fendler, J. H. Adv. Mater. 2004, 16, 1685–1706
  4. Lalander, C. H.; Zheng, Y.; Dhuey, S.; Cabrini, S.; Bach, U. ACS Nano. 2010, 4, 6153–6161
  5. Morel, A. L.; Boujday, S.; M´ethivier, C.; Krafft, J. M.; Pradier, C. M. Talanta 2011, 85, 35–42
  6. Morel, A. L.; Volmant, R. M.; M´ethivier, C.; Krafft, J. M.; Boujday, S.; Pradier, C. M. Colloid. Surface B 2010, 81, 304–312
  7. He, L.; Musick, M. D.; Nicewarner, S. R.; Salinas, F. G.; Benkovic, S. J.; Natan, M. J.; Keating, C. D. J. Am. Chem. Soc. 2000, 122, 9071–9077
  8. Ma, Z.; Sui, S. F. Angew. Chem. Int. Edit. 2002, 41, 2176–2179
  9. Chen, H.; Kou, X.; Yang, Z.; Ni, W.; Wang, J. Langmuir 2008, 24, 5233–5237
  10. Willets, K. A.; Van Duyne, R. P. Annu. Rev. Phys. Chem. 2007, 58, 267–297
  11. Yonzon, C. R.; Stuart, D. A.; Zhang, X.; McFarland, A. D.; Haynes, C. L.; Van Duyne, R. P. Talanta 2005, 67, 438–448
  12. Haes, A. J.; Chang, L.; Klein, W. L.; Van Duyne, R. P. J. Am. Chem. Soc. 2005, 127, 2264–2271
  13. Dahlin, A. B.; Tegenfeldt, J. O.; H¨o¨ok, F. Anal. Chem. 2006, 78, 4416–4423
  14. Stuart, D. A.; Haes, A. J.; McFarland, A. D.; Nie, S.; Van Duyne, R. P. Proceedings of SPIE-The International Society for Optical Engineering 2004, 5327, 60–73
  15. Yonzon, C. R.; Jeoung, E.; Zou, S.; Schatz, G. C.; Mrksich, M.; Van Duyne, R. P. J. Am. Chem. Soc. 2004, 126, 12669–12676
  16. Haes, A. J.; Van Duyne, R. P. J. Am. Chem. Soc. 2002, 124, 10596–10604
  17. Green, N. M. In Advances in Protein Chemistry; Anfinsen, C. B; Edsall, J. T.; Richards, F. M., Eds.; Academic Press: New York, NY, USA, 1975; Vol. 29, p 85–133
  18. Chuang, Y.; Lee, C. Y.; Lu, S. H.; Wang, S. C.; Chau, L. K.; Hsieh, W. H. Anal. Chem. 2010, 82, 1123–1127
  19. Kajiura, M.; Nakanishi, T.; Lida, H.; Takada, H.; Osaka, T. J. Colloid. Interf. Sci. 2009, 335, 140–145
  20. Zhu, S.; Li, F.; Du, C.; Fu, Y. Nanomedicine 2008, 3, 669–677
  21. Wan, M.; Luo, P.; Jin, J.; Xing, J.; Wang, Z.; Wong, S. T. C. Sensors 2010, 10, 6477–6487
  22. Vazquez Mena, O.; Sannomiya, T.; Villanueva, L. G.; Voros, J.; Brugger, J. ACS Nano 2010, 5, 844–853
  23. Lin, Y.; Zou, Y.; Mo, Y.; Guo, J.; Lindquist, R. G. Sensors 2010, 10, 9397–9406
  24. Lin, Y.; Zou, Y.; Lindquist, R. G. Biomed. Opt. Express. 2011, 2, 478–484
  25. Kaur, K.; Forrest, J. A. Langmuir 2011, 28, 2