Review

Surface plasmon resonance for high-throughput ligand screening of membrane-bound proteins

  1. Jennifer A. Maynard Dr.1,
  2. Nathan C. Lindquist2,
  3. Jamie N. Sutherland1,
  4. Antoine Lesuffleur2,
  5. Arthur E. Warrington3,
  6. Moses Rodriguez Professor3,
  7. Sang-Hyun Oh Dr.1,*

Article first published online: 13 NOV 2009

DOI: 10.1002/biot.200900195

Issue

Biotechnology Journal

Biotechnology Journal

Special Issue: Focus: Biochips

Volume 4, Issue 11, pages 1542–1558, November 2009

Additional Information

How to Cite

Maynard, J. A., Lindquist, N. C., Sutherland, J. N., Lesuffleur, A., Warrington, A. E., Rodriguez, M. and Oh, S.-H. (2009), Surface plasmon resonance for high-throughput ligand screening of membrane-bound proteins. Biotechnology Journal, 4: 1542–1558. doi: 10.1002/biot.200900195

Author Information

  1. 1

    Department of Chemical Engineering, University of Texas at Austin, Austin, TX, USA

  2. 2

    Department of Electrical and Computer Engineering, University of Minnesota, Twin Cities, Minneapolis, MN, USA

  3. 3

    Departments of Neurology, Mayo Clinic College of Medicine, Rochester, MN, USA

*Department of Electrical and Computer Engineering, University of Minnesota, Twin Cities, Minneapolis, MN 55455, USA

Publication History

  1. Issue published online: 13 NOV 2009
  2. Article first published online: 13 NOV 2009
  3. Manuscript Accepted: 5 OCT 2009
  4. Manuscript Revised: 28 SEP 2009
  5. Manuscript Received: 15 AUG 2009

Funded by

  • NIH. Grant Number: NS RO1 32129, NS RO1 24180
  • National Multiple Sclerosis Society. Grant Number: R63172, CA 1011A8
  • Applebaum and Hilton Foundations

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Keywords:

  • Autoantibody;
  • G protein-coupled receptor;
  • Membrane protein;
  • Protein array;
  • Surface plasmon resonance

Abstract

Technologies based on surface plasmon resonance (SPR) have allowed rapid, label-free characterization of protein-protein and protein-small molecule interactions. SPR has become the gold standard in industrial and academic settings, in which the interaction between a pair of soluble binding partners is characterized in detail or a library of molecules is screened for binding against a single soluble protein. In spite of these successes, SPR is only beginning to be adapted to the needs of membrane-bound proteins which are difficult to study in situ but represent promising targets for drug and biomarker development. Existing technologies, such as BIAcoreTM, have been adapted for membrane protein analysis by building supported lipid layers or capturing lipid vesicles on existing chips. Newer technologies, still in development, will allow membrane proteins to be presented in native or near-native formats. These include SPR nanopore arrays, in which lipid bilayers containing membrane proteins stably span small pores that are addressable from both sides of the bilayer. Here, we discuss current SPR instrumentation and the potential for SPR nanopore arrays to enable quantitative, high-throughput screening of G protein coupled receptor ligands and applications in basic cellular biology.

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