The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Direct optical sensing of single unlabelled proteins and super-resolution imaging of their binding sites
Open accessAbstract
Detection of single analyte molecules without the use of any label would improve the sensitivity of current biosensors by orders of magnitude to the ultimate graininess of biological matter. Over two decades, scientists have succeeded in pushing the limits of optical detection to single molecules using fluorescence. However, restrictions in photophysics and labelling protocols make this technique less attractive for biosensing. Recently, mechanisms based on vibrational spectroscopy, photothermal detection, plasmonics and microcavities have been explored for fluorescence-free detection of single biomolecules. Here, we show that interferometric detection of scattering (iSCAT) can achieve this goal in a direct and label-free fashion. In particular, we demonstrate detection of cancer marker proteins in buffer solution and in the presence of other abundant proteins. Furthermore, we present super-resolution imaging of protein binding with nanometer localization precision. The ease of iSCAT instrumentation promises a breakthrough for label-free studies of interactions involving proteins and other small biomolecules. The development of biosensors with improved sensitivity for the detection of biological molecules presents obvious possibilities for improved diagnostic tools in healthcare. Here, the authors present a technique for the label-free detection and super-resolution imaging of single proteins.
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Cites
Imaging Intracellular Fluorescent Proteins at Nanometer Resolution
Betzig, E., Patterson, G. H., Sougrat, R., Lindwasser, O. W., Olenych, S., Bonifacino, J. S., Davidson, M. W., Lippincott-Schwartz, J., & Hess, H. F. (2006) · Science · doi:10.1126/science.1127344 · Cited by 8,772
Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
Rust, M. J., Bates, M., & Zhuang, X. (2006) · Nature Methods · doi:10.1038/nmeth929 · Cited by 8,078
Biosensing with plasmonic nanosensors
Anker, J. N., Hall, W. P., Lyandres, O., Shah, N. C., Zhao, J., & Van Duyne, R. P. (2008) · Nature Materials · doi:10.1038/nmat2162 · Cited by 6,786
Surface Plasmon Resonance Sensors for Detection of Chemical and Biological Species
Homola, J. (2008) · Chemical Reviews · doi:10.1021/cr068107d · Cited by 4,525
Cell-free nucleic acids as biomarkers in cancer patients
Schwarzenbach, H., Hoon, D. S. B., & Pantel, K. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3066 · Cited by 2,891
Precise Nanometer Localization Analysis for Individual Fluorescent Probes
Thompson, R. E., Larson, D. R., & Webb, W. W. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75618-x · Cited by 2,320
Ronkainen, N. J., Halsall, H. B., & Heineman, W. R. (2010) · Chemical Society Reviews · doi:10.1039/b714449k · Cited by 1,945
Chemical mapping of a single molecule by plasmon-enhanced Raman scattering
Zhang, R., Zhang, Y., Dong, Z. C., Jiang, S., Zhang, C., Chen, L. G., Zhang, L., Liao, Y., Aizpurua, J., Luo, Y., et al. (2013) · Nature · doi:10.1038/nature12151 · Cited by 1,770
Biosensors: sense and sensibility
Turner, A. P. F. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35528d · Cited by 1,654
Light scattering and the absolute characterization of macromolecules
Wyatt, P. J. (1993) · Analytica Chimica Acta · doi:10.1016/0003-2670(93)80373-s · Cited by 1,436
Single Molecules Observed by Near-Field Scanning Optical Microscopy
Betzig, E., & Chichester, R. J. (1993) · Science · doi:10.1126/science.262.5138.1422 · Cited by 1,262
Wide-field subdiffraction imaging by accumulated binding of diffusing probes
Sharonov, A., & Hochstrasser, R. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609643104 · Cited by 1,151
Label-Free, Single-Molecule Detection with Optical Microcavities
Armani, A. M., Kulkarni, R. P., Fraser, S. E., Flagan, R. C., & Vahala, K. J. (2007) · Science · doi:10.1126/science.1145002 · Cited by 1,141
Borisov, S. M., & Wolfbeis, O. S. (2008) · Chemical Reviews · doi:10.1021/cr068105t · Cited by 1,018
Comparative advantages of mechanical biosensors
Arlett, J. L., Myers, E. B., & Roukes, M. L. (2011) · Nature Nanotechnology · doi:10.1038/nnano.2011.44 · Cited by 966
Zijlstra, P., Paulo, P. M. R., & Orrit, M. (2012) · Nature Nanotechnology · doi:10.1038/nnano.2012.51 · Cited by 788
Lindfors, K., Kalkbrenner, T., Stoller, P., & Sandoghdar, V. (2004) · Physical Review Letters · doi:10.1103/physrevlett.93.037401 · Cited by 571
Self-citationVollmer, F., & Yang, L. (2012) · nanoph · doi:10.1515/nanoph-2012-0021 · Cited by 546
Movement of myosin-coated fluorescent beads on actin cables in vitro
Sheetz, M. P., & Spudich, J. A. (1983) · Nature · doi:10.1038/303031a0 · Cited by 511
Kleinman, S. L., Ringe, E., Valley, N., Wustholz, K. L., Phillips, E., Scheidt, K. A., Schatz, G. C., & Van Duyne, R. P. (2011) · Journal of the American Chemical Society · doi:10.1021/ja110964d · Cited by 427
Vaisocherová, H., Yang, W., Zhang, Z., Cao, Z., Cheng, G., Piliarik, M., Homola, J., & Jiang, S. (2008) · Analytical Chemistry · doi:10.1021/ac8015888 · Cited by 409
Self-citationHigh-speed nanoscopic tracking of the position and orientation of a single virus
Kukura, P., Ewers, H., Müller, C., Renn, A., Helenius, A., & Sandoghdar, V. (2009) · Nature Methods · doi:10.1038/nmeth.1395 · Cited by 390
Self-citationSingle Unlabeled Protein Detection on Individual Plasmonic Nanoparticles
Ament, I., Prasad, J., Henkel, A., Schmachtel, S., & Sönnichsen, C. (2012) · Nano Letters · doi:10.1021/nl204496g · Cited by 335
Label-Free Detection of Single Protein Using a Nanoplasmonic-Photonic Hybrid Microcavity
Dantham, V. R., Holler, S., Barbre, C., Keng, D., Kolchenko, V., & Arnold, S. (2013) · Nano Letters · doi:10.1021/nl401633y · Cited by 305
Ortega-Arroyo, J., & Kukura, P. (2012) · Physical Chemistry Chemical Physics · doi:10.1039/c2cp41013c · Cited by 293
Biosensing with plasmonic nanosensors
ANKER, J. N., HALL, W. P., LYANDRES, O., SHAH, N. C., ZHAO, J., & VAN DUYNE, R. P. (2009) · Nanoscience and Technology · doi:10.1142/9789814287005_0032 · Cited by 272
Cancer biomarkers: selecting the right drug for the right patient
Kelloff, G. J., & Sigman, C. C. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3651 · Cited by 251
Optical Methods for Single Molecule Detection and Analysis
Walt, D. R. (2013) · Analytical Chemistry · doi:10.1021/ac3027178 · Cited by 226
Label-Free, All-Optical Detection, Imaging, and Tracking of a Single Protein
Ortega Arroyo, J., Andrecka, J., Spillane, K. M., Billington, N., Takagi, Y., Sellers, J. R., & Kukura, P. (2014) · Nano Letters · doi:10.1021/nl500234t · Cited by 173
Grading the commercial optical biosensor literature—Class of 2008: ‘The Mighty Binders’
Rich, R. L., & Myszka, D. G. (2010) · Journal of Molecular Recognition · doi:10.1002/jmr.1004 · Cited by 167
Single-molecule approaches to characterizing kinetics of biomolecular interactions
van Oijen, A. M. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.10.002 · Cited by 121
Corrections and Clarifications
(2010) · Science · doi:10.1126/science.328.5985.1480-b · Cited by 109
Manipulating Sticky and Non‐Sticky Properties in a Single Material
Cao, Z., Brault, N. D., Xue, H., Keefe, A. J., & Jiang, S. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201100004 · Cited by 67
Käll, M. (2012) · Nature Nanotechnology · doi:10.1038/nnano.2012.92 · Cited by 26
Taussig, M., & Landegren, U. D. (2003) · TARGETS · doi:10.1016/s1477-3627(03)02345-6 · Cited by 19
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Fein, Y. Y., Geyer, P., Zwick, P., Kiałka, F., Pedalino, S., Mayor, M., Gerlich, S., & Arndt, M. (2019) · Nature Physics · doi:10.1038/s41567-019-0663-9 · Cited by 353
Nanoplasmonic sensors for biointerfacial science
Jackman, J. A., Rahim Ferhan, A., & Cho, N.-J. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00494f · Cited by 258
Interplay between hydrophilicity and surface barriers on water transport in zeolite membranes
Fasano, M., Humplik, T., Bevilacqua, A., Tsapatsis, M., Chiavazzo, E., Wang, E. N., & Asinari, P. (2016) · Nature Communications · doi:10.1038/ncomms12762 · Cited by 123
Metadata
- Authors
- Piliarik, M., & Sandoghdar, V.
- Venue
- Nature Communications
- Published
- 2014-07-29
- Volume
- 5
- Issue
- 1
- Pages
- 4495-4495
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W1819340318
- Cited by
- 332
- References
- 35
- FWCI
- 13.04
- Type
- journal article
- Language
- en
- Open access
- bronze
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