Abstract
We describe a solution-phase sensor of lipid-protein binding based on localized surface plasmon resonance (LSPR) of silver nanocubes. When silica-coated nanocubes are mixed in a suspension of lipid vesicles, supported membranes spontaneously assemble on their surfaces. Using a standard laboratory spectrophotometer, we calibrated the LSPR peak shift due to protein binding to the membrane surface and then characterized the lipid-binding specificity of a pleckstrin homology domain protein.
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Acknowledgements
This work was supported by the Director, Office of Science, Office of Basic Energy Sciences, of the US Department of Energy under contract no. DE-AC02-05CH11231 (to J.T.G.) and by US National Institutes of Health Research Grant GM21841 (to J.T.). P.Y. would like to acknowledge the support from King Abdulaziz University.
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H.-J.W. and J.T.G. conceived the solution-phase nanocube sensor strategy. H.-J.W. implemented the experiments, J.H. synthesized nanocubes and performed TEM, W.-C.L. performed FCS measurements, C.R. performed LSPR simulations and Z.L. and E.S. prepared Ste5 proteins. H.-J.W., C.R. and J.T.G. wrote the manuscript. J.T.G., J.T. and P.Y. supervised the project. All authors discussed the results and commented on the manuscript at all stages.
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Supplementary Figures 1–8, Supplementary Table 1 and Supplementary Discussion (PDF 1434 kb)
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Wu, HJ., Henzie, J., Lin, WC. et al. Membrane-protein binding measured with solution-phase plasmonic nanocube sensors. Nat Methods 9, 1189–1191 (2012). https://doi.org/10.1038/nmeth.2211
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DOI: https://doi.org/10.1038/nmeth.2211
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