Enhanced biomolecular detection based on localized surface plasmon resonance (LSPR) using enzyme-precipitation reaction

Journal of Nanoscience and Nanotechnology

Volumn 10, Issue 5, 2010, Pages 3246-3249

  Lee, Seung Woo ^a,b   Ahn, Junhyoung ^a,b   Kim, Min Gon ^a,b   Shin, Yong Beom ^a,b   Lee, Jae Jong ^b,c   Lim, Ki Pil ^d   Kim, Ki Bum ^d  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b University of Science and Technology (UST)   (South Korea)

^c Korea Institute of Machine and Materials   (South Korea)

^d Seoul National University   (South Korea)

Author keywords

Biosensing; Enzyme Catalyzed precipitation; Localized surface plasmon; Nanodot; Nanoimprint lithography (NIL)

Indexed keywords

ALKALINE PHOSPHATASE; BINDING PROCESS; BIOCATALYTIC REACTION; BIOMOLECULAR DETECTIONS; BIOSENSING; GLASS WAFER; GOLD NANODOTS; HUMAN INTERLEUKIN; INTERMOLECULAR BINDING; LOCALIZED SURFACE PLASMON; LOCALIZED SURFACE PLASMON RESONANCE; MOLECULAR BINDING; NANO-DOT ARRAYS; NANODOTS; P-TOLUIDINE; PEAK WAVELENGTH; PRECIPITATION REACTION; STREPTAVIDIN; THERMAL NANOIMPRINT LITHOGRAPHY;

ANTIBODIES; ENZYMES; GOLD; NANOSTRUCTURED MATERIALS; PHOSPHATASES; PLASMONS; SURFACE PLASMON RESONANCE;

NANOIMPRINT LITHOGRAPHY;

BIOPOLYMER; METALLOPROTEIN; NANOTUBE;

ARTICLE; CHEMISTRY; EQUIPMENT; EQUIPMENT DESIGN; EVALUATION; GENETIC PROCEDURES; IMMUNOASSAY; INSTRUMENTATION; PRECIPITATION; PROTEIN MICROARRAY; SURFACE PLASMON RESONANCE; ULTRASTRUCTURE;

BIOPOLYMERS; BIOSENSING TECHNIQUES; CHEMICAL PRECIPITATION; EQUIPMENT DESIGN; EQUIPMENT FAILURE ANALYSIS; IMMUNOASSAY; METALLOPROTEINS; NANOTUBES; PROTEIN ARRAY ANALYSIS; SURFACE PLASMON RESONANCE;

EID: 77952540458     PISSN: 15334880     EISSN: None     Source Type: Journal    
DOI: 10.1166/jnn.2010.2266     Document Type: Conference Paper

References (19)

1. E. Ozbay, Science 311, 189 (2006).
2. J. J. Mock, D. R. Smith, and S. Schultz, Nano Lett. 3, 485 (2003).
3. A. D. McFarland and R. P. Van Duyne, Nano Lett. 3, 1057 (2003).
4. I. H. El-Sayed, H. X. Huang, and M. A. El-Sayed, Nano Lett. 5, 829 (2005).
5. S. Norman, T. Andersson, C. G. Granqvist, and O. Hunderi, Phys. Rev. B 18, 674 (1978).
6. O. Hunderi, Surf. Sci. 96, 1 (1980).
7. E. Kretschmann, Z. Phys. 241, 313 (1971).
8. M. Gluodenis, C. Manley, and C. A. Foss, Anal. Chem. 71, 4554 (1999).
9. M. D. Malinsky, K. L. Kelly, G. C. Schatz, and R. P. Van Duyne, J. Am. Chem. Soc. 123, 1471 (2001).
10. N. Nath and A. Chilkoti, Anal. Chem. 74, 504 (2002).
11. F. Frederix, J. Friedt, K. Choi, W. Laureyn, A. Campitelli, D. Mondelaers, G. Maes, and G. Borghs, Anal. Chem. 75, 6894 (2003).
12. M. Lahav, A. Vaskevich, and I. Rubinstein, Langmuir 20, 7365 (2004).
13. A. J. Haes, W. P. Hall, L. Chang, W. L. Klein, and R. P. Van Duyne, Nano lett. 4, 1029 (2004).
14. T. Endo, K. Kerman, N. Nagatani, Y. Takamura, and E. Tamiya, Anal. Chem. 77, 6976 (2005).
15. C. R. Yonzon, D. A. Stuart, X. Zhang, A. D. McFarland, C. L. Haynes, and R. P. Van Duyne, Talanta 67, 438 (2005).
16. X. M. Yan, S. Kwon, A. M. Contreras, J. Bokor, and G. A. Somorjai, Nano Lett. 5, 745 (2005).
17. C. L. Haynes, A. D. McFarland, L. Zhao, R. P. Van Duyne, G. Schatz, L. Gunnarsson, J. Prikulis, B. Kasemo and M. Kail, J. Phys. Chem. B 107, 7337 (2003).
18. M. M. Miller and A. Lazarides, J. Phys. Chem. B 109, 21556 (2005).
19. E. M. Larsson, J. Alegret, M. Kail and D. S. Sutherland, Nano Lett. 7, 1256 (2007).