The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Electrically Facilitated Translocations of Proteins through Silicon Nitride Nanopores: Conjoint and Competitive Action of Diffusion, Electrophoresis, and Electroosmosis
Abstract
Solid-state nanopores bear great potential to be used to probe single proteins; however, the passage of proteins through nanopores was found to be complex, and unexpected translocation behavior with respect to the passage direction, rate, and duration was observed. Here we study the translocation of a model protein (avidin) through silicon nitride nanopores focusing on the electrokinetic effects that facilitate protein transport across the pore. The nanopore zeta potential zeta(pore) and the protein zeta potential zeta(protein) are measured independently as a function of solution pH. Our results reveal that electroosmotic transport may enhance or dominate and reverse electrophoretic transport in nanopores. The translocation behavior is rationalized by accounting for the charging states of the protein and the pore, respectively; the resulting translocation direction can be predicted according to the difference in zeta potentials, zeta(protein) - zeta(pore). When electrophoresis and electroosmosis cancel each other out, diffusion becomes an effective (and bias-independent) mechanism which facilitates protein transport across the pore at a significant rate.
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Cites
Microfluidics: Fluid physics at the nanoliter scale
Squires, T. M., & Quake, S. R. (2005) · Reviews of Modern Physics · doi:10.1103/revmodphys.77.977 · Cited by 4,379
The potential and challenges of nanopore sequencing
Branton, D., Deamer, D. W., Marziali, A., Bayley, H., Benner, S. A., Butler, T., Di Ventra, M., Garaj, S., Hibbs, A., Huang, X., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt.1495 · Cited by 2,534
Zeta Potential in Colloid Science
(1981) · Elsevier eBooks · doi:10.1016/c2013-0-07389-6 · Cited by 2,328
Dekker, C. (2007) · Nature Nanotechnology · doi:10.1038/nnano.2007.27 · Cited by 1,933
Transport phenomena in nanofluidics
Schoch, R. B., Han, J., & Renaud, P. (2008) · Reviews of Modern Physics · doi:10.1103/revmodphys.80.839 · Cited by 1,933
Fabrication of solid-state nanopores with single-nanometre precision
Storm, A. J., Chen, J. H., Ling, X. S., Zandbergen, H. W., & Dekker, C. (2003) · Nature Materials · doi:10.1038/nmat941 · Cited by 1,364
Nanopore analytics: sensing of single molecules
Howorka, S., & Siwy, Z. (2009) · Chemical Society Reviews · doi:10.1039/b813796j · Cited by 1,170
Kirby, B. J., & Hasselbrink, E. F. (2004) · ELECTROPHORESIS · doi:10.1002/elps.200305754 · Cited by 1,004
Streaming Currents in a Single Nanofluidic Channel
van der Heyden, F. H. J., Stein, D., & Dekker, C. (2005) · Physical Review Letters · doi:10.1103/physrevlett.95.116104 · Cited by 543
Ionic Selectivity of Single Nanochannels
Vlassiouk, I., Smirnov, S., & Siwy, Z. (2008) · Nano Letters · doi:10.1021/nl800949k · Cited by 456
Cited by
Digitally encoded DNA nanostructures for multiplexed, single-molecule protein sensing with nanopores
Bell, N. A. W., & Keyser, U. F. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.50 · Cited by 345
Doane, T. L., Chuang, C.-H., Hill, R. J., & Burda, C. (2012) · Accounts of Chemical Research · doi:10.1021/ar200113c · Cited by 346
Huber, P. (2015) · Journal of Physics: Condensed Matter · doi:10.1088/0953-8984/27/10/103102 · Cited by 322
Influence of Electroosmotic Flow on Stochastic Collisions at Ultramicroelectrodes
Thorgaard, S. N., Jenkins, S., & Tarach, A. R. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02889 · Cited by 38
Metadata
- Authors
- Firnkes, M., Pedone, D., Knezevic, J., Döblinger, M., & Rant, U.
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-05-03
- Volume
- 10
- Issue
- 6
- Pages
- 2162-2167
- ISSN
- 1530-6984 (ISSN-L)
- 1530-6992
- OpenAlex
- W1964752817
- Cited by
- 473
- References
- 23
- FWCI
- 16.02
- Type
- journal article
- Language
- en
- Open access
- closed
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- Firnkes, M., Pedone, D., Knezevic, J., Döblinger, M., & Rant, U. (2010). Electrically Facilitated Translocations of Proteins through Silicon Nitride Nanopores: Conjoint and Competitive Action of Diffusion, Electrophoresis, and Electroosmosis. Nano Letters. https://doi.org/10.1021/nl100861c
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