journal article·2015-12Open access

Optimizing Nanoplasmonic Biosensor Sensitivity with Orientated Single Domain Antibodies

Marc P. Raphael, Joseph A. Christodoulides, Jeff M. Byers, George P. Anderson, Jinny L. Liu, Kendrick B. Turner, Ellen R. Goldman, James B. Delehanty

Plasmonics· Volume 10· Issue 6

Abstract

Localized surface plasmon resonance (LSPR) spectroscopy and imaging are emerging biosensor technologies which tout label-free biomolecule detection at the nanoscale and ease of integration with standard microscopy setups. The applicability of these techniques can be limited by the restrictions that surface-conjugated ligands must be both sufficiently small and orientated to meet analyte sensitivity requirements. We demonstrate that orientated single domain antibodies (sdAb) can optimize nanoplasmonic sensitivity by comparing three anti-ricin sdAb constructs to biotin-neutravidin, a model system for small and highly orientated ligand studies. LSPR imaging of electrostatically orientated sdAb exhibited a ricin sensitivity equivalent to that of the biotinylated LSPR biosensors for neutravidin. These results, combined with the facts that sdAb are highly stable and readily produced in bacteria and yeast, build a compelling case for the increased utilization of sdAbs in nanoplasmonic applications.
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Research context

OpenAlex topics: Monoclonal and Polyclonal Antibodies Research · Nanofabrication and Lithography Techniques · Advanced Biosensing Techniques and Applications

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

References (35)

Show source-provided references
1. Endo T, Kerman K, Nagatani N, Takamura Y, Tamiya E (2005) Label-free detection of peptide nucleic acid-DNA hybridization using localized surface plasmon resonance based optical biosensor. Anal Chem 77(21):6976–6984. doi: 10.1021/ac051345910.1021/ac0513459 ↗
2. Park JH, Byun JY, Mun H, Shim WB, Shin YB, Li T, Kim MG (2014) A regeneratable, label-free, localized surface plasmon resonance (LSPR) aptasensor for the detection of ochratoxin A. Biosens Bioelectron 59:321–327. doi: 10.1016/j.bios.2014.03.05910.1016/j.bios.2014.03.059 ↗
3. Haes AJ, Van Duyne RP (2002) A nanoscale optical blosensor: sensitivity and selectivity of an approach based on the localized surface plasmon resonance spectroscopy of triangular silver nanoparticles. J Am Chem Soc 124(35):10596–10604. doi: 10.1021/ja020393x10.1021/ja020393x ↗
4. Sepulveda B, Angelome PC, Lechuga LM, Liz-Marzan LM (2009) LSPR-based nanobiosensors. Nano Today 4(3):244–251. doi: 10.1016/j.nantod.2009.04.00110.1016/j.nantod.2009.04.001 ↗
5. Dahlin AB, Jonsson MP, Hook F (2008) Specific self-assembly of single lipid vesicles in nanoplasmonic apertures in gold. Adv Mater 20(8):1436. doi: 10.1002/adma.20070169710.1002/adma.200701697 ↗
6. Endo T, Yamamura S, Kerman K, Tamiya E (2008) Label-free cell-based assay using localized surface plasmon resonance biosensor. Anal Chim Acta 614(2):182–189. doi: 10.1016/j.aca.2008.03.02210.1016/j.aca.2008.03.022 ↗
7. Oh BR, Huang NT, Chen WQ, Seo JH, Chen PY, Cornell TT, Shanley TP, Fu JP, Kurabayashi K (2014) Integrated nanoplasmonic sensing for cellular functional immunoanalysis using human blood. ACS Nano 8(3):2667–2676. doi: 10.1021/nn406370u10.1021/nn406370u ↗
8. Raphael MP, Christodoulides JA, Delehanty JB, Long JP, Byers JM (2013) Quantitative imaging of protein secretions from single cells in real time. Biophys J 105(3):602–608. doi: 10.1016/j.bpj.2013.06.02210.1016/j.bpj.2013.06.022 ↗
9. Wang S, Ota S, Guo B, Ryu J, Rhodes C, Xiong Y, Kalim S, Zeng L, Chen Y, Teitell MA, Zhang X (2011) Subcellular resolution mapping of endogenous cytokine secretion by nano-plasmonic-resonator sensor array. Nano Lett 11(8):3431–3434. doi: 10.1021/nl201883810.1021/nl2018838 ↗
10. Wimalasena RL, Wilson GS (1991) Factors affecting the specific activity of immobilized antibodies and their biologically-active fragments. J Chromatogr Biomed Appl 572(1–2):85–102. doi: 10.1016/0378-4347(91)80475-r10.1016/0378-4347(91)80475-R ↗
11. Haes AJ, Zou SL, Schatz GC, Van Duyne RP (2004) A nanoscale optical biosensor: the long range distance dependence of the localized surface plasmon resonance of noble metal nanoparticles. J Phys Chem B 108(1):109–116. doi: 10.1021/jp036132710.1021/jp0361327 ↗
12. Rindzevicius T, Alaverdyan Y, Kall M, Murray WA, Barnes WL (2007) Long-range refractive index sensing using plasmonic nanostructures. J Phys Chem C 111(32):11806–11810. doi: 10.1021/jp072564w10.1021/jp072564w ↗
13. Bagci H, Kohen F, Kuscuoglu U, Bayer EA, Wilchek M (1993) Monoclonal anti-biotin antibodies simulate avidin in the recognition of biotin. FEBS Lett 322(1):47–50. doi: 10.1016/0014-5793(93)81108-c10.1016/0014-5793(93)81108-C ↗
14. Soler M, Estevez MC, Alvarez M, Otte MA, Sepulveda B, Lechuga LM (2014) Direct detection of protein biomarkers in human fluids using site-specific antibody immobilization strategies. Sensors 14(2):2239–2258. doi: 10.3390/s14020223910.3390/s140202239 ↗
15. Byun JY, Shin YB, Li T, Park JH, Kim DM, Choi DH, Kim MG (2013) The use of an engineered single chain variable fragment in a localized surface plasmon resonance method for analysis of the C-reactive protein. Chem Commun 49(82):9497–9499. doi: 10.1039/c3cc45046e10.1039/c3cc45046e ↗
16. Bonroy K, Frederix F, Reekmans G, Dewolf E, De Palma R, Borghs G, Declerck P, Goddeeris B (2006) Comparison of random and oriented immobilisation of antibody fragments on mixed self-assembled monolayers. J Immunol Methods 312(1–2):167–181. doi: 10.1016/j.jim.2006.03.00710.1016/j.jim.2006.03.007 ↗
17. Chen HX, Huang JY, Lee J, Hwang S, Koh K (2010) Surface plasmon resonance spectroscopic characterization of antibody orientation and activity on the calixarene monolayer. Sens Actuators B 147(2):548–553. doi: 10.1016/j.snb.2010.03.03310.1016/j.snb.2010.03.033 ↗
18. Lu B, Xie JM, Lu CL, Wu CG, Wei Y (1995) Oriented immobilization of Fab' fragments on silica surfaces. Anal Chem 67(1):83–87. doi: 10.1021/ac00097a01410.1021/ac00097a014 ↗
19. Shen ZH, Yan HP, Zhang Y, Mernaugh RL, Zeng XQ (2008) Engineering peptide linkers for scFv immunosensors. Anal Chem 80(6):1910–1917. doi: 10.1021/ac701862410.1021/ac7018624 ↗
20. Torrance L, Ziegler A, Pittman H, Paterson M, Toth R, Eggleston I (2006) Oriented immobilisation of engineered single-chain antibodies to develop biosensors for virus detection. J Virol Methods 134(1–2):164–170. doi: 10.1016/j.jviromet.2005.12.01210.1016/j.jviromet.2005.12.012 ↗
21. Trilling AK, Beekwilder J, Zuilhof H (2013) Antibody orientation on biosensor surfaces: a minireview. Analyst 138(6):1619–1627. doi: 10.1039/c2an36787d10.1039/c2an36787d ↗
22. Vareiro MLM, Liu J, Knoll W, Zak K, Williams D, Jenkins ATA (2005) Surface plasmon fluorescence measurements of human chorionic gonadotrophin: role of antibody orientation in obtaining enhanced sensitivity and limit of detection. Anal Chem 77(8):2426–2431. doi: 10.1021/ac048246010.1021/ac0482460 ↗
23. Trilling AK, Hesselink T, van Houwelingen A, Cordewener JHG, Jongsma MA, Schoffelen S, van Hest JCM, Zuilhof H, Beekwilder J (2014) Orientation of llama antibodies strongly increases sensitivity of biosensors. Biosens Bioelectron 60:130–136. doi: 10.1016/j.bios.2014.04.01710.1016/j.bios.2014.04.017 ↗
24. Walper SA, Lee PAB, Goldman ER, Anderson GP (2013) Comparison of single domain antibody immobilization strategies evaluated by surface plasmon resonance. J Immunol Methods 388(1–2):68–77. doi: 10.1016/j.jim.2012.11.01410.1016/j.jim.2012.11.014 ↗
25. Walper SA, Lee PAB, Anderson GP, Goldman ER (2013) Selection and characterization of single domain antibodies specific for Bacillus anthracis spore proteins. Antibodies 2:152–16710.3390/antib2010152 ↗
26. Turner KB, Zabetakis D, Legler P, Goldman ER, Anderson GP (2014) Isolation and epitope mapping of staphylococcal enterotoxin B single-domain antibodies. Sensors 14(6):10846–10863. doi: 10.3390/s14061084610.3390/s140610846 ↗
27. Anderson G, Liu J, Hale M, Bernstein R, Moore M, Swain M, Goldman E (2008) Development of antiricin single domain antibodies toward detection and therapeutic reagents. Anal Chem 80(24):9604–9611. doi: 10.1021/ac801939810.1021/ac8019398 ↗
28. Anderson G, Bernstein R, Swain M, Zabetakis D, Goldman E (2010) Binding kinetics of antiricin single domain antibodies and improved detection using a B chain specific binder. Anal Chem 82(17):7202–7207. doi: 10.1021/ac100961x10.1021/ac100961x ↗
29. Raphael MP, Christodoulides JA, Mulvaney SP, Miller MM, Long JP, Byers JM (2012) A new methodology for quantitative LSPR biosensing and imaging. Anal Chem 84(3):1367–1373. doi: 10.1021/ac202326610.1021/ac2023266 ↗
30. Goldman ER, Brozozog-Lee PA, Zabetakis D, Turner KB, Walper SA, Liu JL, Anderson GP (2014) Negative tail fusions can improve ruggedness of single domain antibodies. Protein Expr Purif 95:226–232. doi: 10.1016/j.pep.2014.01.00310.1016/j.pep.2014.01.003 ↗
31. Oshea EK, Lumb KJ, Kim PS (1993) Peptide velcro—design of a heterodimeric coiled-coil. Curr Biol 3(10):658–667. doi: 10.1016/0960-9822(93)90063-t10.1016/0960-9822(93)90063-T ↗
32. Goldman ER, Anderson GP, Brozozog-Lee PA, Zabetakis D (2013) SdAb heterodimer formation using leucine zippers. In: Conference on Sensing Technologies for Global Health, Military Medicine, and Environmental Monitoring III, Baltimore, MD, Apr 29-May 01 2013. Proceedings of SPIE 8723. Spie-Int Soc Optical Engineering, BELLINGHAM. doi: 10.1117/12.201614510.1117/12.2016145 ↗
33. Liu JL, Zabetakis D, Walper SA, Goldman ER, Anderson GP (2014) Bioconjugates of rhizavidin with single domain antibodies as bifunctional immunoreagents. J Immunol Methods 411:37–42. doi: 10.1016/j.jim.2014.06.00410.1016/j.jim.2014.06.004 ↗
34. Raphael MP, Christodoulides JA, Delehanty JB, Long JP, Pehrsson PE, Byers JM (2013) Quantitative LSPR imaging for biosensing with single nanostructure resolution. Biophys J 104(1):30–36. doi: 10.1016/j.bpj.2012.11.382110.1016/j.bpj.2012.11.3821 ↗
35. Stenberg E, Persson B, Roos H, Urbaniczky C (1991) Quantitative-determination of surface concentration of protein with surface-plasmon resonance using radiolableled proteins. J Colloid Interface Sci 143(2):513–526. doi: 10.1016/0021-9797(91)90284-f10.1016/0021-9797(91)90284-F ↗