Antibody-functionalised gold nanoparticles-based impedimetric immunosensor: detection methods for better sensitivity

Nadra Bohli; Meryem Belkilani; Laurence Mora; Adnane Abdelghani

Antibody-functionalised gold nanoparticles-based impedimetric immunosensor: detection methods for better sensitivity

View Fulltext

Author(s): Nadra Bohli¹ ; Meryem Belkilani^{1, 2} ; Laurence Mora³ ; Adnane Abdelghani¹
- Affiliations: 1: Carthage University, National Institute of Applied Science and Technology, Research Unit of Nanobiotechnology and Valorisation of Medicinal Plants UR17ES22 , Bp 676 , Centre Urbain Nord , 1080 Charguia Cedex , Tunisia ;
  2: Tunis University , ENSIT, Avenu Taha Hussein, Montfleury, 1008 Tunis , Tunisia ;
  3: Université Paris13, Institut Galilée, Sorbonne Paris Cité , F-93430 Villetaneuse , France
Source: Volume 14, Issue 6, 29 May 2019, p. 629 – 633
DOI: 10.1049/mnl.2018.5587 , Online ISSN 1750-0443

Received 25/09/2018, Accepted 11/02/2019, Revised 20/01/2019, Published 29/05/2019

Electrochemical immunosensors are generally layer-by-layer or sandwich systems designed to detect an analyte in a solution. Immunosensors are mainly based on the high affinity and specificity of the antibody towards its antigen. This work aims to answer the following question: if we ‘flip’ the immunosensor and build it backwards, thus detecting the antibody with the antigen instead of detecting the antigen with the antibody, will we obtain the same immunosensors properties or not? To answer this question, they tested a system composed of glycated human serum albumin and antibody-functionalised gold nanoparticles. Impedance spectrum results showed a difference in both the sensitivity and linear range of the built impedimetric immunosensors. The sensitivity of the sensor using the antibody as a bioreceptor was approximated to 0.32 [%. [% (Glycated to total albumin])] − 1] against a sensitivity of 0.80 [%. [% (Glycated to total albumin])] − 1] for the ‘upside-down’ sensor, using the antigen as a bioreceptor. This study observed also a shift to high glycation levels in the linear range of the upside-down sensor. These differences could be explained by the effect of steric hindrance and a higher degree of freedom allowing better characteristics for the upside-down immunosensor.

References

1. 1)
  - 25. Baraka-Vidot, J., Planesse, C., Meilhac, O., et al: ‘Glycation alters ligand binding, enzymatic, and pharmacological properties of human albumin’, Biochemistry, 2015, 54, pp. 3051–3062 (doi: 10.1021/acs.biochem.5b00273).
2. 2)
  - 16. Cho, I-H., Lee, J., Kim, J., et al: ‘Review current technologies of electrochemical immunosensors: perspective on signal amplification’, Sensors, 2018, 18, p. 207 (doi: 10.3390/s18010207).
3. 3)
  - 3. Perumal, V., Hashim, U.: ‘Advances in biosensors: principle, architecture and applications’, J. Appl. Biomed., 2014, 121, p. 15.
4. 4)
  - 11. Wen, W., Yan, X., Zhu, C., et al: ‘Recent advances in electrochemical immunosensors’, Anal. Chem., 2017, 89, pp. 138–156 (doi: 10.1021/acs.analchem.6b04281).
5. 5)
  - 1. Bahadır, E.B., Sezgintürk, M.K.: ‘Applications of electrochemical immunosensors for early clinical diagnostics’, Talanta, 2015, 132, pp. 162–174 (doi: 10.1016/j.talanta.2014.08.063).
6. 6)
  - 17. Iost, R. M., Crespilho, F. N.: ‘Layer-by-layer self-assembly and electrochemistry: applications in biosensing and bioelectronics’, Biosens. Bioelectron., 2012, 31, pp. 1–10 (doi: 10.1016/j.bios.2011.10.040).
7. 7)
  - 6. Makaraviciute, A., Ramanaviciene, A.: ‘Site-directed antibody immobilization techniques for immunosensors’, Biosens. Bioelectron., 2013, 50, pp. 460–471 (doi: 10.1016/j.bios.2013.06.060).
8. 8)
  - 2. Thevenot, D. R., Toth, K., Durst, R. A., et al: ‘Electrochemical biosensors: recommended definitions and classification’, Anal. Lett., 2001, 34, pp. 635–659 (doi: 10.1081/AL-100103209).
9. 9)
  - 15. Lim, S. A., Ahmed, M. U.: ‘Electrochemical immunosensors and their recent nanomaterial-based signal amplification strategies: a review’, RSC Adv., 2016, 6, (30), pp. 24995–25014 (doi: 10.1039/C6RA00333H).
10. 10)
  - 14. Farka, Z., Juřík, T., Kovář, D., et al: ‘Nanoparticle-based immunochemical biosensors and assays: recent advances and challenges’, Chem. Rev., 2017, 117, pp. 9973–10042 (doi: 10.1021/acs.chemrev.7b00037).
11. 11)
  - 24. Baccar, H., Mejri, M.B., Hafaiedh, I., et al: ‘Surface plasmon resonance immunosensor for bacteria detection’, Talanta, 2010, 82, pp. 810–814 (doi: 10.1016/j.talanta.2010.05.060).
12. 12)
  - 9. Welch, N. G., Scoble, J. A., Muir, B. W., et al: ‘Orientation and characterization of immobilized antibodies for improved immunoassays: review’, Biointerphases, 2017, 12, p. 02D301 (doi: 10.1116/1.4978435).
13. 13)
  - 20. Radecka, H., Radecki, J.: ‘Label-free electrochemical immunosensors for viruses and antibodies detection-review’, J. Mex. Chem. Soc., 2015, 59, (4), pp. 269–275.
14. 14)
  - 18. Wang, Y., Zhang, Y., Wu, D., et al: ‘Ultrasensitive label-free electrochemical immunosensor based on multifunctionalized graphene nanocomposites for the detection of alpha fetoprotein’, Sci. Rep., 2017, 7, p. 42361 (doi: 10.1038/srep42361).
15. 15)
  - 22. Jana, N. R., Gearheart, L., Murphy, C. J.: ‘Seeding growth for size control of 5-40 nm diameter gold nanoparticles’, Langmuir, 2001, 17, pp. 6782–6786 (doi: 10.1021/la0104323).
16. 16)
  - 8. Trilling, A. K., Beekwilder, J., Zuilhof, H.: ‘Antibody orientation on biosensor surfaces: a minireview’, Analyst, 2013, 138, pp. 1619–1627 (doi: 10.1039/c2an36787d).
17. 17)
  - 26. Bohli, N., Meilhac, O., Rondeau, P., et al: ‘A facile route to glycated albumin detection’, Talanta, 2018, 184, pp. 507–512 (doi: 10.1016/j.talanta.2018.03.027).
18. 18)
  - 19. Chammem, H., Hafaid, I., Bohli, N., et al: ‘A disposable electrochemical sensor based on protein G for high-density lipoprotein (HDL) detection’, Talanta, 2015, 144, pp. 466–473 (doi: 10.1016/j.talanta.2015.06.009).
19. 19)
  - 10. Luppa, P. B., Sokoll, L. J., Chan, D. W.: ‘Immunosensors–principles and applications to clinical chemistry’, Clin. Chim. Acta., 2001, 314, pp. 1–26 (doi: 10.1016/S0009-8981(01)00629-5).
20. 20)
  - 12. Khashayar, P., Amoabediny, G., Larijani, B., et al: ‘Fabrication and verification of conjugated AuNP-antibody nanoprobe for sensitivity improvement in electrochemical biosensors’, Sci. Rep., 2017, 7, p. 16070 (doi: 10.1038/s41598-017-12677-w).
21. 21)
  - 4. Santos, A., Davis, J. J., Bueno, P. R.: ‘Fundamentals and applications of impedimetric and redox capacitive biosensors’, J. Anal. Bioanal. Tech., 2014, S7, p. 16 (doi: 10.4172/2155-9872.S7-016).
22. 22)
  - 21. Andresen, H., Mager, M., Grießner, M., et al: ‘Single-step homogeneous immunoassays utilizing epitope-tagged gold nanoparticles: On the mechanism, feasibility, and limitations’, Chem. Mater., 2014, 26, pp. 4696–4704 (doi: 10.1021/cm500535p).
23. 23)
  - 5. Ricci, F., Adornetto, G., Palleschi, G.: ‘A review of experimental aspects of electrochemical immunosensors’, Electrochim. Acta, 2012, 84, pp. 74–83 (doi: 10.1016/j.electacta.2012.06.033).
24. 24)
  - 29. Bhakta, S. A., Evans, E., Benavidez, T. E., et al: ‘Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: A review’, Anal. Chim. Acta., 2015, 872, pp. 7–25 (doi: 10.1016/j.aca.2014.10.031).
25. 25)
  - 28. Bohli, N., Chammem, H., Meilhac, O., et al: ‘Electrochemical impedance spectroscopy on interdigitated gold microelectrodes for glycosylated human serum albumin characterization’, IEEE Trans. NanoBiosci., 2017, 16, pp. 676–681 (doi: 10.1109/TNB.2017.2752693).
26. 26)
  - 23. Jana, N. R., Gearheart, L., Obare, S. O. J., et al: ‘Anisotropic chemical reactivity of gold spheroids and nanorods’, Langmuir, 2002, 18, pp. 922–927 (doi: 10.1021/la0114530).
27. 27)
  - 7. Gopinath, S. C. B., Tang, T.-H., Citartan, M., et al: ‘Current aspects in immunosensors’, Biosens. Bioelectron., 2014, 57, pp. 292–302 (doi: 10.1016/j.bios.2014.02.029).
28. 28)
  - 13. Heddle, J. G.: ‘Gold nanoparticle-biological molecule interactions and catalysis’, Catalysts, 2013, 3, pp. 683–708 (doi: 10.3390/catal3030683).
29. 29)
  - 27. Barsoukov, E., Macdonald, J. R.: ‘Impedance spectroscopy: theory, experiment, and applications’ (Wiley, New York, 2005, 2nd edn.).
30. 30)
  - 30. Kaur, K., Forrest, J. A.: ‘Influence of particle size on the binding activity of proteins adsorbed onto gold nanoparticles’, Langmuir, 2012, 28, pp. 2736–2744 (doi: 10.1021/la203528u).

Login

Not registered yet?

Share

Tools

Login to add to favourites

Key

Antibody-functionalised gold nanoparticles-based impedimetric immunosensor: detection methods for better sensitivity

References

Related content