TY - JOUR
T1 - Surface plasmon resonance for high-throughput ligand screening of membrane-bound proteins
AU - Maynard, Jennifer A.
AU - Lindquist, Nathan C.
AU - Sutherland, Jamie N.
AU - Lesuffleur, Antoine
AU - Warrington, Arthur E.
AU - Rodriguez, Moses
AU - Oh, Sang Hyun
PY - 2009/11
Y1 - 2009/11
N2 - 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 BIAcore™, 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.
AB - 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 BIAcore™, 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.
KW - Autoantibody
KW - G protein-coupled receptor
KW - Membrane protein
KW - Protein array
KW - Surface plasmon resonance
UR - http://www.scopus.com/inward/record.url?scp=73449109166&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=73449109166&partnerID=8YFLogxK
U2 - 10.1002/biot.200900195
DO - 10.1002/biot.200900195
M3 - Review article
C2 - 19918786
AN - SCOPUS:73449109166
SN - 1860-6768
VL - 4
SP - 1542
EP - 1558
JO - Biotechnology Journal
JF - Biotechnology Journal
IS - 11
ER -