Abstract
Almost two decades had passed since the first biosensor based on surface plasmon resonance (SPR) had become commercially available. Among them, the Biacore is the most widely used SPR-based system. More than 10,000 papers, which reported the results obtained using the Biacore (GE Healthcare), had been published until 2015. The most notable progress in the Biacore in this decade is marked reduction of the noise level, which enabled acquisition of the thermodynamic parameters, application to the low molecular weight analytes, observation of the thermodynamic parameters for the activated state, and analysis using further complicate binding model. This chapter aims to provide guidance to users of SPR, with an emphasis on acquiring the thermodynamic parameters for the molecular interaction of two-state binding mechanism, the system exhibiting the interconversion between the transient and the stable complex. No attempt will be made to describe the routine operation and maintenance of the Biacore, as this is comprehensively described elsewhere (Nagata K, Handa H (eds), Real-time analysis of biomolecular interactions: application of BIACORE. Springer, Tokyo, 2000).
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Abbreviations
- AGE:
-
Advanced glycation end product
- CDR:
-
Complementarity-determining region
- GA:
-
Glycolaldehyde
- IgG:
-
Immunoglobulin G
- ITC:
-
Isothermal titration calorimeter
- RU:
-
Resonance unit
- scFv:
-
Single-chain variable fragment
- SPR:
-
Surface plasmon resonance
- VH :
-
Variable region of immunoglobulin heavy chain
- VL :
-
Variable region of immunoglobulin light chain
References
Nagata K, Handa H (eds) (2000) Real-time analysis of biomolecular interactions: application of BIACORE. Springer, Tokyo
Tsumoto K, Yokota A, Tanaka Y, Ui M, Tsumuraya T, Fujii I, Kumagai I, Nagumo Y, Oguri H, Inoue M, Hirama M (2008) Critical contribution of aromatic rings to specific recognition of polyether rings: the case of ciguatoxin CTX3C-ABC and its specific antibody 1C49. J Biol Chem 283:12259–12266
Edink E, Rucktooa P, Retra K, Akdemir A, Nahar T, Zuiderveld O, van Elk R, Janssen E, van Nierop P, van Muijlwijk-Koezen J, Smit AB, Sixma TK, Leurs R, de Esch IJ (2011) Fragment growing induces conformational changes in acetylcholine-binding protein: a structural and thermodynamic analysis. J Am Chem Soc 133:5363–5371
Madura F, Rizkallah PJ, Miles KM, Holland CJ, Bulek AM, Fuller A, Schauenburg AJ, Miles JJ, Liddy N, Sami M, Li Y, Hossain M, Baker BM, Jakobsen BK, Sewell AK, Cole DK (2013) T-cell receptor specificity maintained by altered thermodynamics. J Biol Chem 288:18766–18775
Suzuki N, Tsumoto K, Hajicek N, Daigo K, Tokita R, Minami S, Kodama T, Hamakubo T, Kozasa T (2009) Activation of leukemia-associated RhoGEF by Galpha13 with significant conformational rearrangements in the interface. J Biol Chem 284:5000–5009
Walsh ST (2010) A biosensor study indicating that entropy, electrostatics, and receptor glycosylation drive the binding interaction between interleukin-7 and its receptor. Biochemistry 49:8766–8778
Futamura M, Dhanasekaran P, Handa T, Phillips MC, Lund-Katz S, Saito H (2005) Two-step mechanism of binding of apolipoprotein E to heparin: implications for the kinetics of apolipoprotein E-heparan sulfate proteoglycan complex formation on cell surfaces. J Biol Chem 280:5414–5422
Lipschultz CA, Li Y, Smith-Gill S (2000) Experimental design for analysis of complex kinetics using surface plasmon resonance. Methods 20:310–318
Nagai R, Hayashi CM, Xia L, Takeya M, Horiuchi S (2002) Identification in human atherosclerotic lesions of GA-pyridine, a novel structure derived from glycolaldehyde-modified proteins. J Biol Chem 277:48905–48912
Greven WL, Waanders F, Nagai R, van den Heuvel NC, Navis G, van Goor H (2005) Mesangial accumulation of GA-pyridine, a novel glycolaldehyde-derived AGE, in human renal disease. Kidney Int 68:595–602
Acknowledgments
This work was partly supported by the Grants-in-Aid for Scientific Research (YK and HM) and the Grant-in-Aid for Scientific Research on Innovative Areas (HM) from the Ministry of Education, Culture, Sports, Science and Technology, Japan.
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Kobashigawa, Y., Fukuda, N., Nakahara, Y., Morioka, H. (2016). Surface Plasmon Resonance. In: Senda, T., Maenaka, K. (eds) Advanced Methods in Structural Biology. Springer Protocols Handbooks. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56030-2_13
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DOI: https://doi.org/10.1007/978-4-431-56030-2_13
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