Time-Resolved Fluorometric Method for One-Step Immunoassays Using Plasmonic Nanostructures
Source abstract
Abstract
The use of plasmonic nanostructures for the detection of interactions between biomolecules is currently a very active field of research. In this report, we demonstrate that localized surface plasmons of metallic particles provide the opportunity for sensitive detection of protein−protein interactions in one-step fluoroimmunoassays. Glass coated with silver island films was used for the construction of a bioactive sensing surface where binding results in fluorescence intensity amplification and highly decreased lifetime of the bound probes. The one-step fluoroimmunoassay is demonstrated for detection of TNF-α using a secondary antibody labeled with DY488 dye. Kinetic and end-point measurements were performed using intensity and lifetime (phase shift and modulation) measurements. The ability to vary the ratio of bound to unbound probes provides a mean to tune the assay sensitivity using lifetime measurement modalities. The estimated enhancement in sensitivity is about 100-fold compared to the standard glass surface assay because of intensity amplification of 10.4-fold and similar lifetime decrease. The discussion of experimental results is supported with theoretical calculations with specific parameters for TNF-α assay and DY488 fluorophore. The combined effects of plasmonic structures on intensity and lifetime of fluorophores and the use of phase-modulation fluorometry open the opportunity for bioassay design with high sensitivities and simplified biochemical procedures.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Plasmonic and Surface Plasmon Research · Monoclonal and Polyclonal Antibodies Research · Advanced biosensing and bioanalysis techniques
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Center for Fluorescence Spectroscopy, Department of Biochemistry and Molecular Biology, University of Maryland Baltimore, 725 West Lombard Street, Baltimore, Maryland 21201, and Pierce Biotechnology, Inc., 3747 North Meridian Road, Rockford, Illinois 61101
References (37)
Show source-provided references
1. Haes A. J. · J. Am. Chem. Soc. · 2002 · 124 · 1059610.1021/ja020393x ↗
2. Nath N. · Anal. Chem. · 2002 · 74 · 50410.1021/ac015657x ↗
3. Riboh J. C. · J. Phys. Chem. B · 2003 · 107 · 177210.1021/jp022130v ↗
4. Chen C.-D. · Biosens. Bioelectron. · 2007 · 22 · 92610.1016/j.bios.2006.03.021 ↗
5. Marinakos S. M. · Anal. Chem. · 2007 · 79 · 527810.1021/ac0706527 ↗
6. Frederix F. · Anal. Chem. · 2003 · 75 · 689410.1021/ac0346609 ↗
7. Haes A. J. · J. Am. Chem. Soc. · 2005 · 127 · 226410.1021/ja044087q ↗
8. Endo T. · Anal. Chem. · 2006 · 78 · 646510.1021/ac0608321 ↗
9. Gish D. A. · J. Anal. Chem. · 2007 · 79 · 422810.1021/ac0622274 ↗
10. Mayer K. M. · ACS Nano · 2008 · 2 · 68710.1021/nn7003734 ↗
11. Huang L. · Biosens. Bioelectron. · 2005 · 21 · 48310.1016/j.bios.2004.11.016 ↗
12. Weitz D. A. · J. Chem. Phys. · 1983 · 78 · 532410.1063/1.445486 ↗
13. Kummerlen J. · Mol. Phys. · 1993 · 80 · 103110.1080/00268979300102851 ↗
14. Sokolov K. · Anal. Chem. · 1998 · 70 · 389810.1021/ac9712310 ↗
15. Gerber S. · Phys. Rev. B · 2007 · 75 · 07340410.1103/PhysRevB.75.073404 ↗
16. Lakowicz J. R. · Anal. Biochem. · 2002 · 301 · 26110.1006/abio.2001.5503 ↗
17. Seelig J. · Nano Lett. · 2007 · 7 · 68510.1021/nl0627590 ↗
18. Malicka J. · J. Fluoresc. · 2002 · 12 · 43510.1023/A:1021370111590 ↗
19. Stich N. · J. Nanosci. Nanotechnol. · 2001 · 1 · 39710.1166/jnn.2001.054 ↗
20. Lochner N. · Eur. J. Pharm. Biopharm. · 2003 · 56 · 46910.1016/S0939-6411(03)00115-2 ↗
21. Hong B. · Biosens. Bioelectron. · 2006 · 21 · 133310.1016/j.bios.2005.04.007 ↗
22. Sabanayagan C. R. · Nucleic Acids Res. · 2007 · 35 · e1310.1093/nar/gkl1054 ↗
23. Matveeva E. G. · Anal. Biochem. · 2007 · 361 · 23910.1016/j.ab.2007.01.030 ↗
24. Hsieh B.-Y. · Anal. Chem. · 2007 · 79 · 348710.1021/ac0624389 ↗
25. Malicka J. · Anal. Biochem. · 2003 · 317 · 13610.1016/S0003-2697(03)00005-8 ↗
26. Lukomska J. · J. Fluoresc. · 2004 · 14 · 41710.1023/B:JOFL.0000031823.04926.75 ↗
27. Ditlbacher H. · Appl. Phys. B · 2001 · 73 · 37310.1007/s003400100700 ↗
28. Szmacinski H. · Biotechnol. Bioeng. · 2008 · 100 · 44810.1002/bit.21795 ↗
29. Ni F. · Anal. Chem. · 1986 · 58 · 315910.1021/ac00127a053 ↗
30. Sipior J. · Rev. Sci. Instrum. · 1996 · 67 · 379510.1063/1.1147279 ↗
31. Szmacinski H. · Appl. Spectrosc. · 2000 · 54 · 10610.1366/0003702001948187 ↗
32. Lakowicz, J. R.Principles of Fluorescence Spectroscopy,3rd Edition;Springer Science:New York, 2006; pp.158−204.10.1007/978-0-387-46312-4 ↗
33. Findlay J. W. A. · J. Pharm. Biomed. Anal. · 2000 · 21 · 124910.1016/S0731-7085(99)00244-7 ↗
34. Clegg R. M. · Methods Enzymol. · 1992 · 211 · 35310.1016/0076-6879(92)11020-J ↗
35. Hemmila I. A. · 1991
36. Schneider B. H. · Biosens. Bioelectron. · 2000 · 15 · 1310.1016/S0956-5663(00)00056-7 ↗
37. Vareiro M. M. L. M. · Anal. Chem. · 2005 · 77 · 242610.1021/ac0482460 ↗