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Plasmonics

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A Detailed Study on the Fabrication of Surface Plasmon Sensor Chips: Optimization of Dextran Molecular Weight

  • Ozra Tabasi
  • Cavus FalamakiEmail author
  • Maryam Mahmoudi
Article
  • 35 Downloads

Abstract

The present work discusses a detailed study of the fabrication steps of carboxymethyl-dextran SPR sensor chips with specal focus on the effect of dextran molecular weight (40, 200, and 500 kDa) both on the chip physical characteristics after each fabrication step and on toxin detection performance. Physical characterization was performed using ATR-FTIR, AFM, profilometry, and surface plasmon resonance (SPR) as analytical methods. Based on ATR-FTIR spectroscopy analysis, it is demonstrated that NaOH concentration plays a critical role in the epichlorohydrin (ECH) activation step for subsequent dextran molecules covalent bonding and should be less than 0.4 M, preferably 0.2 M. This is in contrast to the concentration of 0.4 M used in conventional protocols. After covalent binding of the monoclonal anti-staphylococcal enterotoxin B (anti-SEB) to the carboxyl groups of dextran matrix, the detection of enterotoxin B as a function of dextran molecular weight has been assessed. Dextran with a molecular weight of 200 kDa results in a distinct larger SPR angle shift of the final chip with respect to 40 and 500 kDa molecular weights. This observation is explained based on the SPR theory and the physico-chemical characteristics of the antibody/dextran layers measured throughout this study. The SPR sensor chip with the dextran molecular weight of 200 kDa may be considered as an appropriate candidate for the detection of proteins with the same molecular weight as enterotoxin B.

Keywords

SPR sensor chip Carboxymethyl-dextran Detection Enterotoxin B 

Notes

Compliance with Ethical Standards

Conflict of Interest

The authors declare that they have no conflict of interest.

References

  1. 1.
    Yanga W, Chou Chau Y-F, Jheng S-C (2013) Analysis of transmittance properties of surface plasmon modes on periodic solid/outline bowtie nanoantenna arrays. Phys Plasmas 20:064503CrossRefGoogle Scholar
  2. 2.
    Chau Y-F, Jiang Z-H, Li H-Y, Lin G-M, Wu F-L, Lin W-H (2011) Localized resonance of composite core-shell nanospheres, nanobars and nanospherical chains. Prog Electromagn Res 28:183–199CrossRefGoogle Scholar
  3. 3.
    Chau Y-F (2009) Surface plasmon effects excited by the dielectric hole in a silver-shell nanospherical pair. Plasmonics 4:253–259CrossRefGoogle Scholar
  4. 4.
    Chou Chau Y-F, Chou Chao C-T, Lim CM, Huang HJ, Chiang H-P (2018) Deploying tunable metal-shell/dielectric core nanorod arrays as the virtually perfect absorber in the near-infrared regime. ACS Omega 3:7508–7516CrossRefGoogle Scholar
  5. 5.
    Kumara NTRN, Chou Chau Y-F, Huang J-W, Huang HJ, Lin C-T, Hai-Pang Chiang H-P (2016) Plasmonic spectrum on 1D and 2D periodic arrays of rod-shape metal nanoparticle pairs with different core patterns for biosensor and solar cell applications. J Opt 18:115003CrossRefGoogle Scholar
  6. 6.
    Chou Chau Y-F, Wang C-K, Shen L, Lim CM, Chiang H-P, Chou Chao C-T, Huang HJ, Lin C-T, Kumara NTRN, Voo NY (2017) Simultaneous realization of high sensing sensitivity and tunability in plasmonic nanostructures arrays. Sci Rep 7:16817CrossRefGoogle Scholar
  7. 7.
    Lai C-H, Wang G-A, Ling T-K, Wang T-J, Chiu P-K, Chou Chau Y-F, Huang C-C, Chiang H-P (2017) Near infrared surface-enhanced Raman scattering based on star-shaped gold/silver nanoparticles and hyperbolic metamaterial. Sci Rep 7:5446CrossRefGoogle Scholar
  8. 8.
    Karlsson R, Roos H, Fagerstam L, Persson B (1994) Kinetic and concentration analysis using BIA technology. Methods 6(2):99–110CrossRefGoogle Scholar
  9. 9.
    Stenberg E, Persson B, Roos H, Urbaniczky C (1991) Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J Colloid Interface Sci 143(2):513–526CrossRefGoogle Scholar
  10. 10.
    Gupta G, Singh PK, Boopathi M, Kamboj DV, Singh B, Vijayaraghavan R (2010) Surface plasmon resonance detection of biological warfare agent staphylococcal enterotoxin B using high affinity monoclonal antibody. Thin Solid Films 519(3):1171–1177CrossRefGoogle Scholar
  11. 11.
    Homola J, Dostalek J, Chen S, Rasooly A, Jiang S, Yee SS (2002) Spectral surface plasmon resonance biosensor for detection of staphylococcal entrotoxin B in milk. Int J Food Microbiol 75(2):61–69CrossRefGoogle Scholar
  12. 12.
    Rasooly L, Rasooly A (1999) Real time biosensor analysis of Staphylococcal enterotoxin A in food. Int J Food Microbiol 49(3):119–127CrossRefGoogle Scholar
  13. 13.
    Sota H, Hasegawa Y, Iwakura M (1998) Detection of conformational changes in an immobilized protein using surface plasmon resonance. Anal Chem 70(10):2019–2024CrossRefGoogle Scholar
  14. 14.
    Mannen T, Yamaguchi S, Honda J, Sugimoto S, Kitayama A, Nagamune T (2001) Observation of charge state and conformational change in immobilized protein using surface plasmon resonance sensor. Anal Biochem 293(2):185–193CrossRefGoogle Scholar
  15. 15.
    Gestwicki JE, Hsieh HV, Pitner JB (2001) Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance. Anal Chem 73(23):5732–5737CrossRefGoogle Scholar
  16. 16.
    Jung SH, Jung JW, Suh IB, Yuk JS, Kim WJ, Choi EY, Kim YM, Ha KS (2007) Analysis of C-reactive protein on amide-linked N-hydroxysuccinimide-dextran arrays with a spectral surface plasmon resonance biosensor for serodiagnosis. Anal Chem 79(15):5703–5710CrossRefGoogle Scholar
  17. 17.
    Zhang R, Tang M, Bowyer A, Eisenthal R, Hubble J (2005) A novel pH- and ionic-strength-sensitive carboxy methyl dextran hydrogel. Biomaterials 26(22):4677–4683CrossRefGoogle Scholar
  18. 18.
    Frazier RA, Matthijs G, Davies MC, Roberts CJ, Schacht E, Tendler SJB (2000) Characterization of protein-resistant dextran monolayers. Biomaterials 21(9):957–966CrossRefGoogle Scholar
  19. 19.
    Lofas S, Johnsson B (1990) A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands. J Chem Soc Chem Commun 21:1526–1528CrossRefGoogle Scholar
  20. 20.
    Lofas S, Johnsson B, Tegendal K, Ronnberg I (1993) Dextran modified gold surfaces for surface plasmon resonance sensors: immunoreactivity of immobilized antibodies and antibody-surface interaction studies. Colloids Surf B 1(2):83–89CrossRefGoogle Scholar
  21. 21.
    Lofas S (1995) Dextran modified self-assembled monolayer surfaces for use in biointeraction analysis with surface plasmon resonance. Pure Appl Chem 67(5):829–834CrossRefGoogle Scholar
  22. 22.
    Roussille L, Brotons G, Ballut L, louarn G, Ausserre D, Ricard-Blum S (2011) Surface characterization and efficiency of a matrix-free and flat carboxylated gold sensor chip for surface plasmon resonance (SPR). Anal Bioanal Chem 401(5):1601–1617CrossRefGoogle Scholar
  23. 23.
    Chen Y, Zheng RS, Zhang DG, Lu YH, Wang P, Ming H, Luo ZF, Kan Q (2011) Bimetallic chips for a surface plasmon resonance instrument. Appl Opt 50(3):387–391CrossRefGoogle Scholar
  24. 24.
    Zynio SA, Samoylov AV, Surovtseva ER, Mirsky VM, Shirshov YM (2002) Bimetallic layers increase sensitivity of affinity sensors based on surface plasmon resonance. Sensors 2:62–70CrossRefGoogle Scholar
  25. 25.
    Yuan XC, Ong BH, Tan YG, Zhang DW, Irawan R, Tjin SC (2006) Sensitivity-stability-optimized surface plasmon resonance sensing with double metal layers. J Opt A Pure Appl Opt 8(11):959–963CrossRefGoogle Scholar
  26. 26.
    Ghorbanpour M, Falamaki C (2012) Micro energy dispersive X-ray fluorescence as a powerful complementary technique for the analysis of bimetallic au/ag/glass nanolayer composites used in surface plasmon resonance sensors. Appl Opt 51(32):7733–7738CrossRefGoogle Scholar
  27. 27.
    Ghorbanpour M, Falamaki C (2013) A novel method for the production of highly adherent Au layers on glass substrates used in surface Plasmon resonance analysis: substitution of Cr or Ti intermediate layers with Ag layer followed by an optimal annealing treatment. J Nanostruct Chem 3(66):1–7Google Scholar
  28. 28.
    Coates J (2000) Interpretation of infrared spectra, a practical approach. In: Encyclopedia of analytical chemistry. John Wiley & Sons Ltd, ChichesterGoogle Scholar
  29. 29.
    Tabasi O, Falamaki C, Khalaj Z (2012) Functionalized mesoporous silicon for targeted drug-delivery. Colloids Surf B 98:18–25CrossRefGoogle Scholar
  30. 30.
    Azodi M, Falamaki C, Mohsenifar A (2011) Sucrose hydrolysis by invertase immobilized on functionalized porous silicon. J Mol Catal B Enzym 69:154–160CrossRefGoogle Scholar
  31. 31.
    Ghorbanpour M, Falamaki C (2014) A novel method for the fabrication of ATPES silanized SPR sensor chips: exclusion of Cr or Ti intermediate layers and optimization of optical/adherence properties. Appl Surf Sci 301:544–550CrossRefGoogle Scholar
  32. 32.
    Patterson WA (1945) Infrared absorption bands characteristic of the oxirane ring. Anal Chem 26:823–835CrossRefGoogle Scholar
  33. 33.
    Kalsi PS (2004) Spectroscopy of organic compounds. New age international (P) Ltd., New DehliGoogle Scholar
  34. 34.
    Mai-ngam K, Kiatpathomchai W, Arunrut N (2014) Molecular self-assembly of mixed comb-like dextran surfactant polymers for SPR virus detection. Carbohydr Polym 112:440–447CrossRefGoogle Scholar
  35. 35.
    Wijaya E, Lenaerts C, Maricot S, Hastanin J, Habraken S, Vilcot JP, Boukherroub R, Szunerits S (2011) Surface plasmon resonance-based biosensors: from the development of different SPR structures to novel surface functionalization strategies. Curr Opin Solid State Mater Sci 15(5):208–224CrossRefGoogle Scholar
  36. 36.
    Tsai WC, Pai PJR (2009) Surface plasmon resonance-based immunosensor with oriented immobilized antibody fragments on a mixed self-assembled monolayer for the determination of staphylococcal enterotoxin B. Mikrochim Acta 166:115–122CrossRefGoogle Scholar
  37. 37.
    Schasfoort RBM, Tudos AJ (2008) Handbook of Surface Plasmon Resonance. RSC publishing, CambridgeCrossRefGoogle Scholar
  38. 38.
    Chen S, Liu L, Zhou J, Jiang S (2003) Controlling antibody orientation on charged self-assembled monolayers. Langmuir 19(7):2859–2864CrossRefGoogle Scholar
  39. 39.
    Karlsson R, Falt A (1997) Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J Immunol Methods 200:121–133CrossRefGoogle Scholar
  40. 40.
    Barnes WL (2006) Surface plasmon–polariton length scales: a route to sub-wavelength optics. J Opt A Pure Appl Opt 8(4):S87–S93CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Chemical Engineering DepartmentAmirkabir University of TechnologyTehranIran
  2. 2.Research Center for Development of Advanced TechnologiesTehranIran

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