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

Surface plasmon resonance for high‐throughput ligand screening of membrane‐bound proteins 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Journal Wiley

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

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References (131)

Publisher
Wiley
Copyright
Copyright © 2009 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1860-6768
eISSN
1860-7314
DOI
10.1002/biot.200900195
pmid
19918786
Publisher site
See Article on Publisher Site

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.

Journal

Biotechnology Journal – Wiley

Published: Nov 1, 2009

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