Abstract
Over the past 20 years, surface plasmon resonance (SPR) has evolved into a very versatile detection method, particularly in bioscience applications. Not only the scientific literature has greatly expanded, but also the various commercial vendors of instrumentation, detection chips, and reagents have emerged. In the scientific sphere, the accent lies more and more on fabrication of nanostructures with interesting optical behavior (plasmonics), while in the R&D area, there are many new miniaturization efforts and combination with other detection methods, such as electrochemistry and quartz crystal microbalance (QCM). The present chapter will focus on the latest developments in making functional biochemical coatings for SPR detection as well as will review the basic theory behind the detection techniques.
Keywords
- Atomic Force Microscopy
- Surface Plasmon Resonance
- Localize Surface Plasmon Resonance
- Gold Colloid
- Gold Surface
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Notes
- 1.
The extinction (E) of a thin film is calculated by the usual relation: \(E = \chi.d = - \ln \left( T \right) = - \ln \left( {I/I_0 } \right)\), where I 0 is the intensity of the incident beam and I that of the transmitted light, T being the transmittance of the film.
- 2.
In the ellipsometric literature, the convention \(\hat n = n - {\rm{j}}k,\) is often used, but then the k-values are expressed as negative numbers.
- 3.
With the use of hydrogel layers on the gold surface, the SPR method is close to affinity chromatography in which the adsorption and desorption can be monitored directly, instead of monitoring the analyte released from the surface with a down-stream detector.
- 4.
- 5.
Svante Arrhenius (1859–1927) was a Swedish scientist, and one of the founders of the science of physical chemistry: originally he was a physicist, but he is often regarded as a chemist. The Arrhenius equation he developed based on the work by J. H. van‘t Hoff. He was also the first to develop a theory of the greenhouse effect caused by carbon dioxide.
- 6.
A recent scan of the literature readily reveals that most studies with direct detection using SPR instrumentation move in the low nanomolar range [18].
References
Kretschmann E (1968) Radioactive decay of non radiative surface plasmons excited by light. Z. Naturforsch A 23a:2135–2136
Ritchie R H, Arakawa E T, Cowan J J, Hamm R N (1968) Surface-plasmon resonance effect in grating diffraction. Phys. Rev. Lett. 21:1530–1533
Kretschmann E (1971) The determination of the optical constants of metals by excitation of surface plasmons. Z. Phys. A 241:313–324
Raether H (1988) Surface Plasmons. Springer-Verlag, Berlin
Nylander C, Lundstrom I, Liedberg B (1983) Surface plasmon resonance for gas detection and biosensing. Sens. Actuators 4:299–304
Homola J (2006) Surface Plasmon Resonance Based Sensors. Springer-Verlag Heidelberg
Schasfoort R B M, Tudos A J (2004) Handbook of Surface Plasmon Resonance. RSC Publishing, Cambridge
Förch R, Schönherr H, Jenkins A T A (Eds) (2009) Surface Design: Applications in Bioscience and Nanotechnology. VCH/Wiley, Weinheim
Faraday M (1857) Experimental relations of gold (and other metals) to light. Phil. Trans. R. Soc. Lond. 147:145–181
Mie G (1908) Beiträge zur Optik trüber Medien, speziell kolloidaler Metallösungen. Ann. Phys. 4:377–445
Hutter E, Fendler J H (2004) Exploitation of localized surface plasmon resonance. Adv. Mater. 16:1685–1706
Stewart M E, Anderton C R, Thompson L B, Maria J, Gray S K, Rogers J A, Nuzzo R G (2008) Nanostructured plasmonic sensors. Chem. Rev. 108:494–521
Born M, Wolf E (1987) Principles of Optics. Pergamon Press, Oxford
Otto A (1968) Excitation of non-radiative surface plasma waves in silver by the method of frustrated total reflection. Z. Phys. 216:398–410
Azzam R M A, Bashara N M (1987) Ellipsometry and Polarised Light. Elsevier, Amsterdam
Sadowski J W, Korhonen I K J, Peltonen J P K (1995) Characterisation of thin films and their structures in surface plasmon resonance measurements. Opt. Eng. 34:2581–2586
Salamon Z, Macleod H A, Tollin G (1997) Surface plasmon resonance spectroscopy as a tool for investigating the biochemical and biophysical properties of membrane protein systems. Part I. & 2. Biochim. Biophys. Acta 1331:117–129, 131–152
Homola J (2008) Surface plasmon resonance sensors for detection of chemical and biological species. Chem. Rev. 108:462–493
Theye M L (1970) Investigation of the optical properties of Au by means of thin semitransparent films. Phys. Rev. B 2:3060–3078
Dold B, Mecke R (1965) Optische Eigenschaften von Edelmetallen, Übergangsmetallen und deren Legierungen im Infrarot (1. Teil). Optik 22:435–446
Heavens O S (1960) Optical properties of thin films. Rep. Prog. Phys. 23:1–675
Schiebener P, Straub J, Levelt-Sengers, J M H, Gallagher J S (1990) Refractive index of water and steam as function of wavelength, temperature and density. J. Phys. Chem. Ref. Data 19:677
Ghosh G (1997) Sellmeier coefficients and dispersion of thermo-optic coefficients for some optical glasses. Appl. Opt. 36:1540–1546
Nelson B P, Frutos A G, Brockman J M, Corn R M (1999) Near-infrared surface plasmon resonance measurements of ultrathin films. 1. Angle shift and SPR imaging experiments. Anal. Chem. 71:3928–3934
De Feijter J A, Benjamins J, Veer F A (1978) Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface. Biopolymers 17:1759–1772
Vörös J (2004) The density and refractive index of adsorbing protein layers. Biophys. J. 87:553–561
Qian R L, Mhatre R, Krull I S (1997) Characterization of antigen-antibody complexes by size-exclusion chromatography coupled with low-angle light-scattering photometry and viscometry. J. Chromatogr. A 787:101–109
Ball V, Ramsden J J (1998) Buffer dependence of refractive index increments. Biopolymers 46:489–492
Arwin H (1986) Optical properties of thin layers of bovine serum albumin, γ-globulin, and hemoglobin. Appl. Spectrosc. 40:313–318
Oudshoorn R C G, Kooyman R P H, Greve J (1996) Refractive index and layer thickness of on adsorbing protein as reporters of monolayer formation. Thin Solid Films 284–285:836–840
Sadowski J W, Lekkala J, Vikholm I (1991) Biosensors based on surface plasmons excited in non-noble metals. Biosens. Bioelectron. 6:439–444
Mayer C, Schalkhammer T (2005) Bioanalytical sensing using noble metal colloids. Top. Fluoresc. Spectrosc. 8:135–195
Kontio J M, Husu H, Simonen J, Huttunen M J, Tommila J, Pessa M, Kauranen M (2009) Source nanoimprint fabrication of gold nanocones with ∼10 nm tips for enhanced optical interactions. Opt. Lett. 34:1979–1981
Dahlin A, Zäch M, Rindzevicius T, Käll M, Sutherland D S, Höök F (2005) Localized surface plasmon resonance sensing of lipid-membrane-mediated biorecognition events. J. Am. Chem. Soc. 127:5043–5048
Turkevich J, Stevenson P C, Hillier J A (1951) Study of the nucleation and growth processes in the synthesis of colloidal gold. Discuss. Faraday. Soc. 11:55–75
Frens G (1973) Controlled nucleation for the regulation of the particle size in monodisperse gold suspension. Nat. Phys. Sci. 241:20–21
Jana N R, Gearheart L, Murphy C J (2001) Evidence for seed-mediated nucleation in the chemical reduction of gold salts to gold nanoparticles. Chem. Mater. 13:2313–2322
Jadzinsky P D, Calero G, Ackerson C J, Bushnell, D A, Kornberg, R D (2007) Structure of a thiol monolayer-protected gold nanoparticle at 1.1 Å resolution. Science 318:430–433
Slot J W, Geuze H J (1985) A new method for preparing gold probes for multiple-labelling cytochemistry. Eur. J. Cell. Biol. 38:87–93
Brust M, Walker M, Bethell D, Schiffrin D J, Whyman R (1994) Synthesis of thiol-derivatised gold nanoparticles in a two-phase liquid–liquid system. J. Chem. Soc. Chem. Commun. 94:801
Link S L, El-Sayed M A (1999) Size and temperature dependence of the plasmon adsorption of colloidal gold nanoparticles. J. Phys. Chem. 103:4212–4217
Creighton J A, Eadon D G (1991) Ultraviolet-visible absorption spectra of the colloidal metallic elements. J. Chem. Soc. Faraday Trans. 87:3881–3891
Englebienne P, Van Hoonacker A, Verhas M (2003) Surface plasmon resonance: principles, methods and applications in biomedical sciences. Spectroscopy 17:255–273
Haiss W, Thanh N T K, Aveyard J, Fernig D G (2007) Determination of size and concentration of gold nanoparticles from UV-Vis spectra. Anal. Chem. 79:4215–4221
Khlebtsov N G (2008) Determination of size and concentration of gold nano-particles from extinction spectra. Anal. Chem. 80:6620–6625
Englebienne P (1998) Use of colloidal gold surface plasmon resonance peak shift to infer affinity constants from the interactions between protein antigens and antibodies specific for single or multiple epitopes. Analyst 123:1599–1603
Gribnau T C J, Leuvering J H W, van Hell H (1986) Particle-labelled immunoassays: a review. J. Chrom. B 376:175–189
Brooks D E, Devine D V, Harris P C, Harris J E, Miller M E, Olal A D, Spiller L J, Xie Z C (1999) RAMP™: a rapid, quantitative whole blood immunochromatographic platform for point-of-care testing. Clin. Chem. 45:1676–1678
Lyon L A, Musick M D, Natan M J (1998) Colloidal Au-enhanced surface plasmon resonance immunosensing. Anal. Chem. 70:5177–5183
Liedberg B, Nylander C, Lundström I (1995) Biosensing with surface plasmon resonance – how it all started. Biosens. Bioelectron. 10:i–ix
McDonnell J M (2001) Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition. Curr. Opin. Chem. Biol. 5:572–577
Arnold F H, Schofield S A, Blanch H W (1986) Analytical affinity chromatography: I. Local equilibrium theory and the measurement of association and inhibition constants. J. Chrom. A 355:1–12 & Arnold F H, Blanch H W (1986) Analytical affinity chromatography: II. Rate theory and the measurement of biological binding kinetics. J. Chrom. A 355:13–27
Cannon M J et al. (2004) Comparative analyses of a small molecule/enzyme interaction by multiple users of Biacore technology. Anal. Biochem. 330:98–113
Katsamba PS et al. (2006) Kinetic analysis of a high-afnity antibody/antigen interaction performed by multiple Biacore users. Anal. Biochem. 352:208–221
Navratilova I et al. (2007) Thermodynamic benchmark study using Biacore technology. Anal. Biochem. 364:67–77
Rich R L (2009) A global benchmark study using affinity-based biosensors. Anal. Biochem. 386:194–216
Karlsson R, Fält A (1997) Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200:121–133
Morton T A, Myszka D G, Chaiken I M (1995) Interpreting complex binding kinetics from optical biosensors: a comparison of analysis by linearization, the integrated rate equation, and numerical integration. Anal. Biochem. 227:176–185
Rich R L, Myszka D G (2010) Grading the commercial optical biosensor literature – class of 2008: “The Mighty Binders”. J Mol. Recognit. 23:1–64
de Crescenzo G, Boucher C, Durocher Y, Jolicoeur M (2008) Kinetic characterization by surface plasmon resonance-based biosensors: principle and emerging trends. Cell. Mol. Bioeng. 1:204–215
Price N, Nairn J (2009) Exploring Proteins: A Student’s Guide to Experimental Skills and Methods. Oxford University Press, Oxford
Sips R (1950) On the structure of a catalyst surface. J. Chem. Phys. 18:1024
García-Calzóna J A, Díaz-García M E (2006) Review: characterization of binding sites in molecularly imprinted polymers. Sens. Actuators B 123:1180–1194
Vijayendran R A, Leckband D E (2001) A quantitative assessment of heterogeneity for surface-immobilized proteins. Anal. Chem. 73:471–480
Selinger J V, Rabbany S Y (1997) Theory of heterogeneity in displacement reactions. Anal. Chem. 69:170–174
Jaroniec M, Madey R (1988) Physical Adsorption on Heterogeneous Solids. Elsevier, Amsterdam
Koopal L K, Vos C H W (1993) Adsorption on heterogeneous surfaces. Calculation of the adsorption energy distribution function or the affinity spectrum. Langmuir 9:2593–2605
Puzly A M, Matynia T, Gawdzik B, Poddubnaya O I (1999) Use of CONTIN for calculation of energy distribution. Langmuir 15:6016–6025
Press W H, Flannery B P, Teukolsky S A, Vetterling W T (1986) Numerical Recipes. Cambridge University Press, New York, p 502
Malmborg A-C, Michaëlsson A, Ohlin M, Jansson b, Borrebäck C A K (1992) Real time analysis of antibody-antigen reaction kinetics. Scand. J. Immunol. 35:643–650
Karlsson R, Katsamba P S, Nordin H, Pol E, Myszka D G (2006) Analyzing a kinetic titration series using affinity biosensors. Anal. Biochem. 349:136–147
Myszka D G, He X, Dembo M, Morton T A, Goldstein B (1998) Extending the range of rate constants available from BIACORE: interpreting mass transport-influenced binding data. Biophys. J. 75:583–594
Önell A, Andersson K (2005) Kinetic determinations of molecular interactions using Biacore-minimum data requirements for efficient experimental design. J. Mol. Recognit. 18:307–317
Svitel J, Boukari H, Van Ryk D, Willson R, Schuck P (2007) Probing the functional heterogeneity of surface binding sites by analysis of experimental binding traces and the effect of mass transport limitation. Biophys. J. 92:1742–1758
Myszka D A, Morton T A (1998) CLAMP: a biosensor kinetic data analysis program. Trends Biochem. Sci. 23:149–150
Lipschultz C A, Li Y, Smith-Gill S (2000) Experimental design for analysis of complex kinetics using surface plasmon resonance. Methods 20:310–318
Myszka D A (1999) Improving biosensor analysis. J Mol. Recognit. 12:279–284
Thevenot D R, Toth K, Durst R A, Wilson G S (1999) Pure Appl. Chem. 71:2333–2348
Wortberg M, Orban M, Renneberg R, Cammann K (1996) Fluorimetric immunosensors. In: Kress-Rogers E (Ed) Handbook of Biosensors and Electronic noses. CRC Press, Boca Raton, p 371
Eddowes M J (1987–1988) Direct immunochemical sensing: basic chemical principles and fundamental limitations. Biosensors 3:1–15
(2003) Biacore 3000 Instrument Handbook. GE Healthcare, Uppsala
Jonsson B, Löfås S, Lindquist G (1991) Immobilization of proteins to carboxy methyl dextran-modified gold surface for biospecific analysis in surface plasmon resonance sensors. Anal. Biochem. 198:268–277
Löfås S, Jönsson B (1992) A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands. J. Chem. Soc. Commun. 21:1526–1528
Kambhampati D (Ed) (2005) Protein Microarray Technology. VCH/Wiley, Weinheim
Boozer C, Kim G, Cong S, Guan H, Londergan T (2006) Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies. Curr. Opin. Biotechnol. 17:400–405
Eddings M A, Eckman J W, Arana C A, Papalia G A, Connolly J E, Gale B. K, Myszka D G (2009) “Spot and hop”: internal referencing for surface plasmon resonance imaging using a three-dimensional microfluidic flow cell array. Anal. Biochem. 385:309–313
Beusink J B, Lokate A M C, Besselink G A J, Pruijn G J M, Schasfoort R B M (2008) Angle-scanning SPR imaging for detection of biomolecular interactions on microarrays. Biosens. Bioelectron. 23:839–844
Albers W M, Vikholm I, Viitala T, Peltonen J (2001) Interfacial and materials aspects of the immobilisation of biomolecules onto solid surfaces. In: Nalwa HS (Ed) Handbook of Surfaces and Interfaces of Materials. Academic Press, San Diegop. p. 1–(1/N)31
Shankaran D R, Miura N (2007) Trends in interfacial design for surface plasmon resonance based immunoassays. J. Phys. D: Appl. Phys. 40:7187–7200
Gutiérrez-Gallego R, Bosch J, Such-Sanmartín G, Segura J (2009) Surface plasmon resonance immunoassays – a perspective. Growth Horm. IGF Res. 19:388–398
Bilitewski U (2006) Review: protein-sensing assay formats and devices. Anal. Chim. Acta 568:232–247
Förch R, Schönherr H, Jenkins A T A (Eds) (2009) Surface Design: Applications in Bioscience and Nanotechnology. Wiley/VCH, Weinheim
Lofas S, Johnsson B, Tegendal K, Ronnberg I (1993) Dextran modified gold surface plasmon resonance sensors: immunoreactivity of immobilized antibodies and antibody–surface interaction studies. Colloids Surf. B 1:83–89
Stigter E C A, de Jong G J, van Bennekom W P (2005) An improved coating for the isolation and quantitation of interferon-γ in spiked plasma using surface plasmon resonance (SPR). Biosens. Bioelectron. 21:474–482
Löfås S (1995) Dextran modified self-assembled monolayer surfaces for use in biointeraction analysis with surface plasmon resonance. Pure Appl. Chem. 67:829–834
Löfås S, Johnsson B, Edström Å, Hansson A, Lindqvist G, Müller-Hillgren R-M, Stigh L (1995) Methods for site controlled coupling to carboxymethyldextran surfaces in surface plasmon resonance sensors. Biosens. Bioelectron. 10:813–822
GE Healthcare (2010) Data sheet No. 28–9681–84 AA, Sensor Chip CM7
Myszka D G (2004) Analysis of small-molecule interactions using Biacore S51 technology. Anal. Biochem. 329:316–323
Rich R L, Day Y S N, Morton T A, Myszka D G (2001) High-resolution and high-throughput protocols for measuring drug/human serum albumin interactions using BIACORE. Anal. Biochem. 296:197–207
Cannon M J, Myszka D G, Bagnato J D, Alpers D H, West F G, Grissom C B (2002) Anal. Biochem. 305:1–9
Rich R L, Hoth L R, Geoghegan K F, Brown T A, LeMotte P K, Simons S P, Hensley P, Myszka D G (2002) Kinetic analysis of estrogen receptor-ligand interactions. Proc. Natl. Acad. Sci. U.S.A. 99:8562–8567
Johnson B, Löfås S, Lindquist G, Edström Å, Müller-Hillgren R-M, Hansson A (1995) Comparison of methods for immobilisation to carboxymethyl dextran sensor surfaces by analysis of the specific activity of monoclonal antibodies. J. Mol. Recognit. 8:125–131
Volden S, Kaizheng Z, Nystrom B, Glomm W R (2009) Use of cellulose derivatives on gold surfaces for reduced nonspecific adsorption of immunoglobulin G. Colloids Surf. B, 72:266–271
Kyprianou D, Guerreiro A R, Chianella I, Piletska E V, Fowler S A, Karim K, Whitcombe M J, Turner A P F, Piletsky S A (2009) New reactive polymer for protein immobilisation on sensor surfaces. Biosens. Bioelectron. 24:1365–1371
Iwasaki Y, Omichi Y, Iwata R (2008) Site-specific dense immobilization of antibody fragments on polymer brushes supported by silicone nanofilaments. Langmuir 24:8427–8430
F. Khan, M. He, M.J. Taussig, Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on ninitrilotriacetic acid surfaces. Anal. Chem. 78 (2006) 3072–3079
Y. Huang, R. Shi, X. Zhong, D. Wang, M. Zhao, Y. Li, Enzyme-linked immunosorbent assays for insulin-like growth factor-I using six-histidine tag fused proteins. Anal. Chim. Acta 596 (2007) 116–123
Morgan H, Taylor D M (1992) A surface plasmon resonance immunosensor based on the streptavidin–biotin complex. Biosens. Bioelectron. 7:405–510
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 312:167–181
Nagatomo K, Kawaguchi T, Miura N, Toko K, Matsumoto K (2009) Development of a sensitive surface plasmon resonance immunosensor for detection of 2,4-dinitrotoluene with a novel oligo (ethylene glycol)-based sensor surface. Talanta 79:1142–1148
Vikholm I, Viitala T, Albers W M, Peltonen J (1999) Highly efficient immobilisation of antibody fragments to functionalised lipid monolayers. Biochim. Biophys. Acta 1421:39–52
Goto Y, Matsuno R, Konno T, Takai M, Ishihara K (2008) Polymer nanoparticles covered with phosphorylcholine groups and immobilized with antibody for high-affinity separation of proteins. Biomacromolecules 9:828–833
Yuan Y, He H, Lee L J (2009) Protein A-based antibody immobilization onto polymeric microdevices for enhanced sensitivity of enzyme-linked immunosorbent assay. Biotechnol. Bioeng. 102:891–901
Lekkala J O, Sadowski J W (1994) Surface plasmon immunosensors. In: Aizawa M (Ed) Chemical Sensor Technology. Kodansha, Tokyo 5:199–213
Oh B K, Lee W, Chun B S, Bae Y M, Lee W H, Choi J W (2005) Surface plasmon resonance immunosensor for the detection of Yersinia enterocolitica. Colloids Surf. A 257–258:369–374
Svensson H G et al. (1998) Protein LA, a novel hybrid protein with unique single-chain Fv antibody- and Fab-binding properties. Eur. J. Biochem. 258:890–896
Kihlberg B M et al. (1992) Protein LG: a hybrid molecule with unique immunoglobulin binding properties. J. Biol. Chem. 267:25583–25588
Saerens D, Huang L, Bonroy K, Muyldermans S (2008) Review: antibody fragments as probe in biosensor development. Sensors. doi:10.3390/s8084669
Vareiro M M, Liu J, Knoll W, Zak K, Williams D, Jenkins A T (2005) Surface Plasmon fluorescence measurements of human chorionic gonadotropin: role of antibody orientation in obtaining enhanced sensitivity and limit of detection. Anal. Chem. 77:2426–2431
Jung Y, Jeong J Y, Chung B H (2008) Recent advances in immobilization methods of antibodies on solid supports. Analyst 133:697–701
O’Brien J C, Jones V W, Porter M D, Mosher C L, Henderson E (2000) Immunosensing platforms using spontaneously adsorbed antibody fragments on gold. Anal. Chem. 72:703–710
Weber J, Albers W M, Tuppurainen J, Link M, Gabl R, Wersing W, Schreiter M (2006) Shear mode FBARs as highly sensitive liquid biosensors. Sens. Actuators A 128:84–88
Albers W M, Auer S, Helle H, Munter T, Vikholm-Lundin I (2009) Functional characterisation of Fab’-fragments self-assembled onto hydrophilic gold surfaces. Colloids Surf. B 68:193–199
Vikholm I (2005) Self-assembly of antibody fragments and polymers onto gold for immunosensing. Sens. Actuators B 106:311–316
Vikholm-Lundin I (2005) Immunosensing based on site-directed immobilization of antibody fragments and polymers that reduce nonspecific binding. Langmuir 21:6473–6477
Vikholm-Lundin I, Albers W M (2006) Site-directed immobilisation of antibody fragments for detection of C-reactive protein. Biosens. Bioelectron. 21:1141–1148
Vikholm I. Sadowski J (2007) Method and biosensor for analysis. US Patent no. 7332327
Zayats M, Pogorelov S P, Kharitonov A B, Lioubashevski O (2003) Au nanoparticle-enhanced surface plasmon resonance sensing of biocatalytic transformations. Chem. Eur. J. 9:6108–6114
Hanning A, Roerade J, Delrow J J, Jorgenson R C (1999) Enhanced sensitivity of wavelength modulated surface plasmon resonance devices using dispersion from a dye solution. Sens. Actuators B 54:25–36
Wink T, Zuilen S J V, Bult A, van Bennekom W P (1998) Liposome-mediated enhancement of the sensitivity in immunoassays of proteins and peptides in surface plasmon resonance spectrometry. Anal. Chem. 70:827–832
Chen S-J, Chien F C, Lin G Y, Lee K C (2004) Enhancement of the resolution of surface plasmon resonance biosensors by control of the size and distribution of nanoparticles. Opt. Lett. 29:1390–1392
Liu X, Sun Y, Song D Q, Zhang Q L, Tian Y, Zhang H Q (2004) Sensitivity-enhancement of wavelength-modulation surface plasmon resonance biosensor for human complement factor 4. Anal. Biochem. 333:99–104
Tian Y, Chen Y H, Song D Q, Liu X, Zhang H Q (2005) Acousto-optic tunable filter-surface plasmon resonance immunosensor for fibronectin, Anal. Chim. Acta 551:98–104
Gobi K V, Sasaki M, Shoyama Y, Miura N (2003) Highly sensitive detection of polycyclic aromatic hydrocarbons (PAHs) and association constants of the interaction between PAHs and antibodies using surface plasmon resonance immunosensor. Sens. Actuators B 89:137–143
Aldinger U, Pfeifer P, Schwotzer G, Steinrucke P (1998) A comparative study of spectral and angle-dependent SPR devices in biological applications. Sens. Actuators B 51:298–304
Besselink G A J, Kooyman R P H, van Os, P J H J, Engbers G H M, Schasfoort, R B M (2004) Signal amplification on planar and gel-type sensor surfaces in surface plasmon resonance-based detection of prostate-specific antigen. Anal. Biochem. 333:165–173
Choi J-W, Kang D-Y, Jang Y-H, Kim H-H, Min J, Oh B-K (2008) Ultra-sensitive surface plasmon resonance based immunosensor for prostate-specific antigen using gold nanoparticle-antibody complex. Colloids Surf. B 313–314:655–659
Mangeney C et al. (2002) Synthesis and properties of water-soluble gold colloids covalently derivatized with neutral polymer monolayers. J. Am. Chem. Soc. 124:5811–5821
Albers W M, Munter T, Laaksonen P, Vikholm-Lundin I (2010) Improved functionality of antibody-colloidal gold conjugates with the aid of lipoamide-grafted N-[tris(hydroxymethyl)methyl]acrylamide polymers. J. Colloid Interface Sci. 348(1):1–8
Fouqu’e B, Schaack B, Obëıd P, Combe S, Gétin S, Barritault P, Chaton P, Chatelein F (2005) Multiple wavelength fluorescence enhancement on glass substrates for biochip and cell analyses. Biosens. Bioelectron. 20:2335–2340
Liu J, Cao Z, Lu Y (2009) Functional nucleic acid sensors. Chem. Rev. 109:1948–1998
Lucarelli F, Tombelli S, Minunni M, Marrazza G, Mascini M (2008) Electrochemical and piezoelectric DNA biosensors for hybridisation detection. Anal. Chim. Acta 609:139–159
Ananthanawat C, Vilaivan T, Mekboonsonglarp W, Hoven V P (2009) Thio-lated pyrrolidinyl peptide nucleic acids for the detection of DNA hybridization using surface plasmon resonance. Biosens. Bioelectron. 24:3544–3549
Liu Y, Wilson W D (2010) Quantitative analysis of small molecule-nucleic acid interactions with a biosensor surface and surface plasmon resonance detection. Methods Mol. Biol. 613:1–23
Torres-Chavolla E, Alocilja E C (2009) Aptasensors for detection of microbial and viral pathogens. Biosens. Bioelectron. 24:3175–3182
Kohlhammer H et al. (2004) Genomic DNA-chip hybridisation in t(11;14)-positive mantle cell lymphomas shows a high frequency of aberrations and allows a refined characterization of consensus regions. Blood 104:795–801
Deng J Y, Zhang X E, Mang Y, Zhang Z P, Zhou Y F, Liu Q, Lu H B, Fu Z J (2004) Oligonucleotide ligation assay-based DNA chip for multiplex detection of single nucleotide polymorphism. Biosens. Bioelectron. 19:1277–1283
Mannelli I, Lecerf L, Guerrouache M, Goossens M, Millot M-C, Canva M (2007) DNA immobilisation procedures for surface plasmon resonance imaging (SPRI) based microarray systems. Biosens. Bioelectron. 22:803–809
Mannelli I, Courtois V, Lecaruyer P, Roger G, Millot M C, Goossens M, Canva M (2006) Surface plasmon resonance imaging (SPRI) system and real-time monitoring of DNA biochip for human genetic mutation diagnosis of DNA amplified samples. Sens. Actuators B 119 583–591
Bianchi N, Rutigliano C, Tomassetti M, Feriotto G, Zorzato F, Gambari R (1997) Biosensor technology and surface plasmon resonance for real-time detection of HIV-1 genomic sequences amplified by polymerase chain reaction. Clin. Diagn. Virol. 8:199–208
Feriotto G, Borgatti M, Mischiati C, Bianchi N, Gambari R (2002) Biosensor technology and surface plasmon resonance for real-time detection of genetically modified roundup ready soybean gene sequences. J. Agric. Food Chem. 50:955–962
Silin V, Plant A (1997) Biotechnological applications of surface plasmon resonance. Tibtech 15:353–359
Nikiforov T T, Rogers Y H (1995) The use of 96-well polystyrene plate for DNA hybridization-based assays: an evaluation of different approaches to oligonucleotide immobilization. Anal. Biochem. 227:201–209
Rehman F N, Audeh M, Abrama E S, Hammond P W, Kenney M, Boles T C (1999) Immobilisation of acrylamide-modified oligonucleotides by co-polymerisation. Nucleic Acids Res. 27:649–655
Nimyer C M, Boldt L, Ceyhan B, Blohm D (1999) DNA-directed immobilization: efficient, reversible, and site-selective surface binding or proteins by means of covalent DNA streptavidin conjugates. Anal. Biochem. 268:54–63
Herne T, Tarlov M (1997) Characterization of DNA probes immobilized on gold surfaces. J. Am. Chem. Soc. 119:8916–8920
Kim J H, Hong J, Yoon M, Yoon M Y, Juong H-S, Hwang H (2002) Solid-phase genetic engineering with DNA immobilized on a gold surface. J. Biotechnol. 96:213–221
Rogers Y H., Jiang-Baucom P, Huang Z J, Bogdanov V, Anderson S, Boyce-Jacino M (1999) Immobilization of oligonucleotides onto glass support via disulfide bonds: a method for preparation of DNA microarrays. Anal. Biochem. 266:23–30
Peterson A, Wolf L, Georgiadis R (2002) Hybridization of mismatched or partially matched DNA at surfaces. J. Am. Chem. Soc. 124:14601–14607
Lucarelli F, Marrazza G, Turner A P F, Mascini M (2004) Carbon and gold electrodes as electrochemical transducers for DNA hybridisation sensors. Biosens. Bioelectron. 19:515–530
Dugas V, Depret G, Chevalier Y, Nesme X, Souteyrand E (2004) Immobilization of single-stranded DNA fragments to solid surfaces and their repeatable specific hybridization: covalent binding or adsorption? Sens. Actuators B 101:112–121
Cloarec J-P, Chevolot Y, Laurenceau E, Phaner-Goutorbe M, Souteyrand E (2008) A multidisciplinary approach for molecular diagnostics based on biosensors and microarrays. ITBM-RBM 29:105–127
Sandström P, Boncheva M, Åkerman B (2003) Nonspecific and thiol-specific binding of DNA to Gold nanoparticles. Langmuir 19:7537–7543
Steel A B, Levicky R L, Herne T M, Tarlov M J (2000) Immobilization of nucleic acids at solid surfaces: effect of oligonucleotide length on layer assembly. Biophys. J. 79:975–981
Steel A, Herne T, Tarlov M (1999) Electrostatic interactions of redox cations with surface-immobilized and solution DNA. Bioconjug. Chem. 10:419–423
Vikholm-Lundin I, Piskonen R, Albers W M (2007) Hybridisation of surface-immobilised single-stranded oligonucleotides and polymer monitored by surface plasmon resonance. Biosens. Bioelectron. 22:1323–1329
Vikholm-Lundin I, Piskonen R (2008) Binary monolayers of single-stranded oligonucleotides and blocking agent for hybridization. Sens. Actuators B 134:189–192
Vikholm-Lundin I, Auer S, Munter T, Fiegl H, Apostolidou S (2009) Hybridization of binary monolayers of single stranded oligonucleotides and short blocking molecules. Surf. Sci. 603:620–624
Morris V J, Kirby A R, Gunning A P (2004) Atomic Force Microscopy for Biologists. Imperial College Press, London
Eaton P, West P (2010) Atomic Force Microscopy. Oxford University Press, Oxford
Watson G S, Watson J (Eds Quantitative Measurements of Nano Forces Using Atomic Force Microscopy (AFM) – Quantifying Nano Forces in Three-Dimensions Using AFM: Applications in the Biological, Physical and Chemical Sciences. VDM Verlag, Saarbrücken
Braga P C, Ricci D (2003) Atomic Force Microscopy: Biomedical Methods and Applications (Methods in Molecular Biology, Vol 242). Humana Press, Totowa NY, USA
Morris V J, Kirby A R, Gunning A P (2010) Atomic Force Microscopy for Biologists. Imperial College Press, London
Zhang Y, Sheng S J, Shao Z (1996) Imaging biological structures with the cryo atomic force microscope. Biophys. J. 71:2168–2176
Hafner J H, Cheung C L, Woolley A T, Lieber C M (2001) Structural and functional imaging with carbon nanotube AFM probes. Prog. Biophys. Mol. Biol. 77:73–110
Hafner J H, Cheung C L, Lieber C M (1999) Growth of nanotubes for probe microscopy tips. Nature (London) 398:761–762
Cheung C L, Hafner J H, Lieber C M (2000) Carbon nanotube atomic force microscopy tips: direct growth by chemical vapour deposition and application to high-resolution imaging. Proc. Natl. Acad. Sci. U.S.A. 97:3809–3813
San Paulo A, Garcia R (2000) High-resolution imaging of antibodies by tapping-mode atomic force microscopy: attractive and repulsive tip-sample interaction regimes. Biophys. J. 78:1599–1605
San Paulo A, Garcia R (2000) High-resolution imaging of antibodies by tapping-mode atomic force microscopy: attractive and repulsive tip-sample interaction regimes. Biophys. J. 78:1599–1605
Thomson N H (2005) The substructure of immunoglobulin G resolved to 25 kDa using amplitude modulation AFM in air. Ultramicroscopy 105:103–110
Zitzler L, Herminghaus S, Mugele F (2002) Capillary forces in tapping mode atomic force microscopy. Phys. Rev. B 66:155436–155443
Thomson N H (2005) Imaging the substructure of antibodies with tapping mode AFM in air: the importance of a water layer on mica. J Microsc. 217:193–199
Lallemand D, Rouillat M H, Dugas V, Chevolot Y, Souteyrand E, Phaner-Goutorbe M (2007) AFM characterization of ss-DNA probes immobilization: a sequence effect on surface organization. J. Phys. Conf. Ser. 61:658–662
Ando T, Uchihashi T, Fukuma T (2008) High-speed atomic force microscopy for nanovisualisation of dynamic biomolecular processes. Prog. Surf. Sci. 83:337–437
Tappura K, Vikholm-Lundin I, Albers W M (2007) Lipoate-based imprinted self-assembled molecular thin films for biosensor applications. Biosens. Bioelectron. 22:912–919
Hoa X D, Kirk A G, Tabrizian (2007) Towards integrated and sensitive surface plasmon resonance biosensors: a review of the recent progress. Biosens. Bioelectron. 23:151–160
Weber J, Albers W M, Tuppurainen J, Link M, Gabl R, Wersing W, Schreiter M (2006) Shear mode FBARs as highly sensitive liquid biosensors. Sens. Actuators A 128:84–88
Acknowledgments
Financial support from VTT Technical Research Centre, the EU, and TEKES in various projects is gratefully acknowledged. We also express thanks to Risto Ahorinta, of ORC, Tampere University of technology, for some ellipsometric measurements reported in this chapter.
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Appendices
Appendix A
The Jones matrix I ifor reflection/transmission at an interface between layer i and i + 1 is based on the Fresnell reflection/transmission coefficients r i and t i, according to:
where in the case of p-polarized light, the coefficients are:
in the case of s-polarised light, the coefficients are:
The Jones matrix L i for the light absorption in layer i takes the form, according to the Lambert-Beer law as:
(when using the convention \(\hat n = n+ ik)\,\) \(where\, c_i = \cos (\theta _i ) = \sqrt {1 - \frac{{\hat n_1^2 }}{{\hat n_i^2 }}\sin ^2 (\theta _1 )}.\)
Appendix B
Reaction Schemes and rate equations for the most frequently used binding systems, from [57] in modified form.
One-to-one reaction
One-to-one reaction with mass transfer
One-to-two reaction (bivalent analyte)
Two-state reaction
Competing analyte
where A and C are the analyte species involved in the reaction, with square brackets indicating their concentration at the surface, and A* denoting species A in the bulk of the solution. B is the immobilized species, and AB, CB, AB’, and A2B are the complexes formed at the surface, with R, R 1, and R 2 are the responses of the bound species, and R max is the maximum response of species B. The parameter p is a correction factor, for example, to account for difference in molecular weight between species A and C. k is the rate constant, with a and d indicating the forward (association) and reverse (dissociation) reaction, and indices 1 and 2 indicating the equation
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Albers, W.M., Vikholm-Lundin, I. (2011). Surface Plasmon Resonance on Nanoscale Organic Films. In: Carrara, S. (eds) Nano-Bio-Sensing. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6169-3_4
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