Measuring Protein Interactions by Optical Biosensors

Peter Schuck1, Lisa F. Boyd1, Peter S. Andersen2

1 National Institutes of Health, Bethesda, Maryland, 2 University of Maryland, Rockville, Maryland
Publication Name:  Current Protocols in Cell Biology
Unit Number:  Unit 17.6
DOI:  10.1002/0471143030.cb1706s22
Online Posting Date:  May, 2004
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Abstract

In recent years, optical evanescent wave biosensors have been used to characterize protein‐protein interactions, including determination of equilibrium binding constants and bimolecular rate constants. This surface binding technique can provide information about chemical on‐rate constants, the lifetimes of complexes formed, and the time course of the signal. This unit provides a thorough, well‐illustrated discussion of the principles of optical biosensors, experimental design, ligand immobilization, experimental data analysis, and common obstacles and possible solutions.

     
 
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Table of Contents

  • Strategic Planning
  • Immobilization Protocols
  • Binding Experiments and Data Analysis
  • Common Experimental Obstacles
  • Summary
  • Acknowledgment
  • Literature Cited
  • Figures
  • Tables
     
 
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Materials

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Figures

Videos

Literature Cited

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   Schuck, P. 1997a. Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. Annu. Rev. Biophys. Biomol. Struct. 26:541‐566.
   Schuck, P. 1997b. Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8:498‐502.
   Schuck, P. and Minton, A.P. 1996a. Minimal requirements for internal consistency of the analysis of surface plasmon resonance biosensor data. Trends Biochem. Sci. 252:458‐460.
   Schuck, P. and Minton, A.P. 1996b. Analysis of mass transport limited binding kinetics in evanescent wave biosensors. Anal. Biochem. 240:262‐272.
   Schuck, P., Millar, D.B., and Kortt, A.A. 1998. Determination of binding constants by equilibrium titration with circulating sample in a surface plasmon resonance biosensor. Anal. Biochem. 265:79‐91.
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   Silhavy, T.J., Szmelcman, S., Boos, W., and Schwartz, M. 1975. On the significance of the retention of ligand by protein. Proc. Natl. Acad. Sci. USA. 72:2120‐2124.
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Key References
   Davis et al, 1998. See above.
  Contains a detailed description of analyte aggregation effects on the measured surface binding.
   Nieba et al., 1996. See above.
  Demonstration how competition approaches can be used to circumvent kinetic artifacts.
   O'Shannessy et al., 1992. See above.
  Collection of immobilization techniques.
   Schuck, 1997b. See above.
  General review of the method and its application.
Internet Resources
   http://www.biacore.com
  Web site for Biacore; extensive list of published biosensor applications
   http://www.affinity‐sensors.com
  Web site for Affinity Sensors; extensive list of published biosensor applications.
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