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Volumn 7, Issue 4, 2012, Pages 257-263

Stochastic sensing of proteins with receptor-modified solid-state nanopores

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; MOLECULES; SILICON NITRIDE; STOCHASTIC SYSTEMS;

EID: 84859583528     PISSN: 17483387     EISSN: 17483395     Source Type: Journal    
DOI: 10.1038/nnano.2012.24     Document Type: Article
Times cited : (435)

References (52)
  • 1
    • 69249086081 scopus 로고    scopus 로고
    • Nanopore analytics: Sensing of single molecules
    • Howorka, S. & Siwy, Z. Nanopore analytics: sensing of single molecules. Chem. Soc. Rev. 38, 2360-2384 (2009).
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2360-2384
    • Howorka, S.1    Siwy, Z.2
  • 2
    • 4143057920 scopus 로고    scopus 로고
    • Atomic layer deposition to fine-tune the surface properties and diameters of fabricated nanopores
    • Chen, P. et al. Atomic layer deposition to fine-tune the surface properties and diameters of fabricated nanopores. Nano Lett. 4, 1333-1337 (2004).
    • (2004) Nano Lett. , vol.4 , pp. 1333-1337
    • Chen, P.1
  • 3
    • 78149415469 scopus 로고    scopus 로고
    • Rapid electronic detection of probe-specific microRNAs using thin nanopore sensors
    • Wanunu, M. et al. Rapid electronic detection of probe-specific microRNAs using thin nanopore sensors. Nature Nanotech. 5, 807-814 (2011).
    • (2011) Nature Nanotech. , vol.5 , pp. 807-814
    • Wanunu, M.1
  • 4
    • 34347212530 scopus 로고    scopus 로고
    • Single-molecule mass spectrometry in solution using a solitary nanopore
    • Robertson, J. W. F. et al. Single-molecule mass spectrometry in solution using a solitary nanopore. Proc. Natl Acad. Sci. USA 104, 8207-8211 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8207-8211
    • Robertson, J.W.F.1
  • 5
    • 34547650531 scopus 로고    scopus 로고
    • Electrical characterization of protein molecules by a solid-state nanopore
    • Fologea, D., Ledden, B., McNabb, D. S. & Li, J. L. Electrical characterization of protein molecules by a solid-state nanopore. Appl. Phys. Lett. 91, 053901 (2007).
    • (2007) Appl. Phys. Lett. , vol.91 , pp. 053901
    • Fologea, D.1    Ledden, B.2    McNabb, D.S.3    Li, J.L.4
  • 6
    • 45249104680 scopus 로고    scopus 로고
    • Label-free detection of single protein molecules and protein-protein interactions using synthetic nanopores
    • Han, A. et al. Label-free detection of single protein molecules and protein-protein interactions using synthetic nanopores. Anal. Chem. 80, 4651-4658 (2008).
    • (2008) Anal. Chem. , vol.80 , pp. 4651-4658
    • Han, A.1
  • 7
    • 67649908631 scopus 로고    scopus 로고
    • Single-molecule protein unfolding in solid state nanopores
    • Talaga, D. S. & Li, J. L. Single-molecule protein unfolding in solid state nanopores. J. Am. Chem. Soc. 131, 9287-9297 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9287-9297
    • Talaga, D.S.1    Li, J.L.2
  • 8
    • 33747166710 scopus 로고    scopus 로고
    • Submicrometer pore-based characterization and quantification of antibody-virus interactions
    • Uram, J. D., Ke, K., Hunt, A. J. & Mayer, M. Submicrometer pore-based characterization and quantification of antibody-virus interactions. Small 2, 967-972 (2006).
    • (2006) Small , vol.2 , pp. 967-972
    • Uram, J.D.1    Ke, K.2    Hunt, A.J.3    Mayer, M.4
  • 9
    • 70349952483 scopus 로고    scopus 로고
    • Translocation of RecA-coated double-stranded DNA through solid-state nanopores
    • Smeets, R. M. M., Kowalczyk, S. W., Hall, A. R., Dekker, N. H. & Dekker, C. Translocation of RecA-coated double-stranded DNA through solid-state nanopores. Nano Lett. 9, 3089-3095 (2009).
    • (2009) Nano Lett. , vol.9 , pp. 3089-3095
    • Smeets, R.M.M.1    Kowalczyk, S.W.2    Hall, A.R.3    Dekker, N.H.4    Dekker, C.5
  • 10
    • 67649206290 scopus 로고    scopus 로고
    • Origin of the electrophoretic force on DNA in solid-state nanopores
    • Van Dorp, S., Keyser, U. F., Dekker, N. H., Dekker, C. & Lemay, S. G. Origin of the electrophoretic force on DNA in solid-state nanopores. Nature Phys. 5, 347-351 (2009).
    • (2009) Nature Phys. , vol.5 , pp. 347-351
    • Van Dorp, S.1    Keyser, U.F.2    Dekker, N.H.3    Dekker, C.4    Lemay, S.G.5
  • 11
    • 77953298585 scopus 로고    scopus 로고
    • Electrically facilitated translocations of proteins through silicon nitride nanopores: Conjoint and competitive action of diffusion, electrophoresis, and electroosmosis
    • Firnkes, M., Pedone, D., Knezevic, J., Doblinger, M. & Rant, U. Electrically facilitated translocations of proteins through silicon nitride nanopores: conjoint and competitive action of diffusion, electrophoresis, and electroosmosis. Nano Lett. 10, 2162-2167 (2010).
    • (2010) Nano Lett. , vol.10 , pp. 2162-2167
    • Firnkes, M.1    Pedone, D.2    Knezevic, J.3    Doblinger, M.4    Rant, U.5
  • 12
    • 65549134365 scopus 로고    scopus 로고
    • Interrogating single proteins through nanopores: Challenges and opportunities
    • Movileanu, L. Interrogating single proteins through nanopores: challenges and opportunities. Trends Biotechnol. 27, 333-341 (2009).
    • (2009) Trends Biotechnol. , vol.27 , pp. 333-341
    • Movileanu, L.1
  • 13
    • 80052258551 scopus 로고    scopus 로고
    • Controlling molecular transport through nanopores
    • Keyser, U. F. Controlling molecular transport through nanopores. J. R. Soc. Interface 8, 1369-1378 (2011).
    • (2011) J. R. Soc. Interface , vol.8 , pp. 1369-1378
    • Keyser, U.F.1
  • 14
    • 34248399955 scopus 로고    scopus 로고
    • Solid-state nanopore channels with DNA selectivity
    • Iqbal, S. M., Akin, D. & Bashir, R. Solid-state nanopore channels with DNA selectivity. Nature Nanotech. 2, 243-248 (2007).
    • (2007) Nature Nanotech. , vol.2 , pp. 243-248
    • Iqbal, S.M.1    Akin, D.2    Bashir, R.3
  • 15
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • Bayley, H. & Cremer, P. S. Stochastic sensors inspired by biology. Nature 413, 226-230 (2001).
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 16
    • 77956171429 scopus 로고    scopus 로고
    • Stochastic nanopore sensors for the detection of terrorist agents: Current status and challenges
    • Liu, A. H., Zhao, Q. T. & Guan, X. Y. Stochastic nanopore sensors for the detection of terrorist agents: current status and challenges. Anal. Chim. Acta 675, 106-115 (2010).
    • (2010) Anal. Chim. Acta , vol.675 , pp. 106-115
    • Liu, A.H.1    Zhao, Q.T.2    Guan, X.Y.3
  • 17
    • 0034424832 scopus 로고    scopus 로고
    • Simultaneous stochastic sensing of divalent metal ions
    • Braha, O. et al. Simultaneous stochastic sensing of divalent metal ions. Nature Biotechnol. 18, 1005-1007 (2000).
    • (2000) Nature Biotechnol. , vol.18 , pp. 1005-1007
    • Braha, O.1
  • 18
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • Gu, L. Q., Braha, O., Conlan, S., Cheley, S. & Bayley, H. Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter. Nature 398, 686-690 (1999).
    • (1999) Nature , vol.398 , pp. 686-690
    • Gu, L.Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 19
    • 0034930381 scopus 로고    scopus 로고
    • Sequence-specific detection of individual DNA strands using engineered nanopores
    • Howorka, S., Cheley, S. & Bayley, H. Sequence-specific detection of individual DNA strands using engineered nanopores. Nature Biotechnol. 19, 636-639 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 636-639
    • Howorka, S.1    Cheley, S.2    Bayley, H.3
  • 20
    • 0033776849 scopus 로고    scopus 로고
    • Detecting protein analytes that modulate transmembrane movement of a polymer chain within a single protein pore
    • Movileanu, L., Howorka, S., Braha, O. & Bayley, H. Detecting protein analytes that modulate transmembrane movement of a polymer chain within a single protein pore. Nature Biotechnol. 18, 1091-1095 (2000).
    • (2000) Nature Biotechnol. , vol.18 , pp. 1091-1095
    • Movileanu, L.1    Howorka, S.2    Braha, O.3    Bayley, H.4
  • 21
    • 34248351114 scopus 로고    scopus 로고
    • Solid-state nanopores
    • Dekker, C. Solid-state nanopores. Nature Nanotech. 2, 209-215 (2007).
    • (2007) Nature Nanotech. , vol.2 , pp. 209-215
    • Dekker, C.1
  • 22
    • 34547190841 scopus 로고    scopus 로고
    • Chemically modified solid-state nanopores
    • Wanunu, M. & Meller, A. Chemically modified solid-state nanopores. Nano Lett. 7, 1580-1585 (2007).
    • (2007) Nano Lett. , vol.7 , pp. 1580-1585
    • Wanunu, M.1    Meller, A.2
  • 23
    • 35848967784 scopus 로고    scopus 로고
    • Resistive-pulse studies of proteins and protein/antibody complexes using a conical nanotube sensor
    • Sexton, L. T. et al. Resistive-pulse studies of proteins and protein/antibody complexes using a conical nanotube sensor. J. Am. Chem. Soc. 129, 13144-13152 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 13144-13152
    • Sexton, L.T.1
  • 24
    • 79955802477 scopus 로고    scopus 로고
    • Controlling protein translocation through nanopores with bioinspired fluid walls
    • Yusko, E. C. et al. Controlling protein translocation through nanopores with bioinspired fluid walls. Nature Nanotech. 6, 253-260 (2011).
    • (2011) Nature Nanotech. , vol.6 , pp. 253-260
    • Yusko, E.C.1
  • 25
    • 79960098185 scopus 로고    scopus 로고
    • Single-molecule transport across an individual biomimetic nuclear pore complex
    • Kowalczyk, S. W. et al. Single-molecule transport across an individual biomimetic nuclear pore complex. Nature Nanotech. 6, 433-438 (2011).
    • (2011) Nature Nanotech. , vol.6 , pp. 433-438
    • Kowalczyk, S.W.1
  • 26
    • 17144391818 scopus 로고    scopus 로고
    • Protein biosensors based on biofunctionalized conical gold nanotubes
    • Siwy, Z. et al. Protein biosensors based on biofunctionalized conical gold nanotubes. J. Am. Chem. Soc. 127, 5000-5001 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5000-5001
    • Siwy, Z.1
  • 27
    • 57149105534 scopus 로고    scopus 로고
    • Biosensing and supramolecular bioconjugation in single conical polymer nanochannels. Facile incorporation of biorecognition elements into nanoconfined geometries
    • Ali, M. et al. Biosensing and supramolecular bioconjugation in single conical polymer nanochannels. Facile incorporation of biorecognition elements into nanoconfined geometries. J. Am. Chem. Soc. 130, 16351-16357 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16351-16357
    • Ali, M.1
  • 29
    • 68849091326 scopus 로고    scopus 로고
    • Capturing single molecules of immunoglobulin and ricin with an aptamer-encoded glass nanopore
    • Ding, S., Gao, C. & Gu, L-Q. Capturing single molecules of immunoglobulin and ricin with an aptamer-encoded glass nanopore. Anal. Chem. 81, 6649-6655 (2009).
    • (2009) Anal. Chem. , vol.81 , pp. 6649-6655
    • Ding, S.1    Gao, C.2    Gu, L.-Q.3
  • 30
    • 77956928026 scopus 로고    scopus 로고
    • Ultrasensitive mycotoxin detection by STING sensors
    • Actis, P., Jejelowo, O. & Pourmand, N. Ultrasensitive mycotoxin detection by STING sensors. Biosens. Bioelectron. 26, 333-337 (2010).
    • (2010) Biosens. Bioelectron. , vol.26 , pp. 333-337
    • Actis, P.1    Jejelowo, O.2    Pourmand, N.3
  • 31
    • 79957698013 scopus 로고    scopus 로고
    • Enantioselective recognition in biomimetic single artificial nanochannels
    • Han, C. P. et al. Enantioselective recognition in biomimetic single artificial nanochannels. J. Am. Chem. Soc. 133, 7644-7647 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7644-7647
    • Han, C.P.1
  • 32
    • 77954301825 scopus 로고    scopus 로고
    • Fabrication of metallized nanopores in silicon nitride membranes for single-molecule sensing
    • Wei, R. S., Pedone, D., Zurner, A., Doblinger, M. & Rant, U. Fabrication of metallized nanopores in silicon nitride membranes for single-molecule sensing. Small 6, 1406-1414 (2010).
    • (2010) Small , vol.6 , pp. 1406-1414
    • Wei, R.S.1    Pedone, D.2    Zurner, A.3    Doblinger, M.4    Rant, U.5
  • 33
    • 77952401811 scopus 로고    scopus 로고
    • An adsorption-based model for pulse duration in resistive-pulse protein sensing
    • Sexton, L. T. et al. An adsorption-based model for pulse duration in resistive-pulse protein sensing. J. Am. Chem. Soc. 132, 6755-6763 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6755-6763
    • Sexton, L.T.1
  • 34
    • 24744472221 scopus 로고    scopus 로고
    • High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: A generic platform for protein chip technologies
    • Tinazli, A. et al. High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: a generic platform for protein chip technologies. Chem. Eur. J. 11, 5249-5259 (2005).
    • (2005) Chem. Eur. J. , vol.11 , pp. 5249-5259
    • Tinazli, A.1
  • 35
    • 27644474237 scopus 로고    scopus 로고
    • Removal of self-assembled monolayers of alkanethiolates on gold by plasma cleaning
    • Raiber, K., Terfort, A., Benndorf, C., Krings, N. & Strehblow, H-H. Removal of self-assembled monolayers of alkanethiolates on gold by plasma cleaning. Surf. Sci. 595, 56-63 (2005).
    • (2005) Surf. Sci. , vol.595 , pp. 56-63
    • Raiber, K.1    Terfort, A.2    Benndorf, C.3    Krings, N.4    Strehblow, H.-H.5
  • 36
    • 12044254336 scopus 로고
    • Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide)-a model system using self-assembled monolayers
    • Prime, K. L. & Whitesides, G. M. Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide)-a model system using self-assembled monolayers. J. Am. Chem. Soc. 115, 10714-10721 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 10714-10721
    • Prime, K.L.1    Whitesides, G.M.2
  • 37
    • 0030077272 scopus 로고    scopus 로고
    • A self-assembled monolayer for the binding and study of histidine tagged proteins by surface plasmon resonance
    • Sigal, G. B., Bamdad, C., Barberis, A., Strominger, J. & Whitesides, G. M. A self-assembled monolayer for the binding and study of histidine tagged proteins by surface plasmon resonance. Anal. Chem. 68, 490-497 (1996).
    • (1996) Anal. Chem. , vol.68 , pp. 490-497
    • Sigal, G.B.1    Bamdad, C.2    Barberis, A.3    Strominger, J.4    Whitesides, G.M.5
  • 38
    • 79960281274 scopus 로고    scopus 로고
    • Stochastic sensing of single molecules in a nanofluidic electrochemical device
    • Zevenbergen, M. A. G., Singh, P. S., Goluch, E. D.,Wolfrum, B. L. & Lemay, S. G. Stochastic sensing of single molecules in a nanofluidic electrochemical device. Nano Lett. 11, 2881-2886 (2011).
    • (2011) Nano Lett. , vol.11 , pp. 2881-2886
    • Zevenbergen, M.A.G.1    Singh, P.S.2    Goluch, E.D.3    Wolfrum, B.L.4    Lemay, S.G.5
  • 39
    • 13844263242 scopus 로고    scopus 로고
    • Stable and functional immobilization of histidine-tagged proteins via multivalent chelator headgroups on a molecular poly(ethylene glycol) brush
    • Lata, S. & Piehler, J. Stable and functional immobilization of histidine-tagged proteins via multivalent chelator headgroups on a molecular poly(ethylene glycol) brush. Anal. Chem. 77, 1096-1105 (2005).
    • (2005) Anal. Chem. , vol.77 , pp. 1096-1105
    • Lata, S.1    Piehler, J.2
  • 40
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves
    • Hill, A. V. The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves. J. Physiol. 40, iv-vii (1910).
    • (1910) J. Physiol. , vol.40
    • Hill, A.V.1
  • 41
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun, D. Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br. J. Pharmacol. 125, 924-947 (1998).
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 42
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • Woodhull, A. M. Ionic blockage of sodium channels in nerve. J. Gen. Physiol. 61, 687-708 (1973).
    • (1973) J. Gen. Physiol. , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 43
    • 0033798636 scopus 로고    scopus 로고
    • Interaction of the noncovalent molecular adapter, β-cyclodextrin, with the staphylococcal a-hemolysin pore
    • Gu, L. Q. & Bayley, H. Interaction of the noncovalent molecular adapter, β-cyclodextrin, with the staphylococcal a-hemolysin pore. Biophys. J. 79, 1967-1975 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 1967-1975
    • Gu, L.Q.1    Bayley, H.2
  • 44
    • 14844318136 scopus 로고    scopus 로고
    • Nanopore unzipping of individual DNA hairpin molecules
    • Mathe, J., Visram, H., Viasnoff, V., Rabin, Y. & Meller, A. Nanopore unzipping of individual DNA hairpin molecules. Biophys. J. 87, 3205-3212 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 3205-3212
    • Mathe, J.1    Visram, H.2    Viasnoff, V.3    Rabin, Y.4    Meller, A.5
  • 45
    • 0033861876 scopus 로고    scopus 로고
    • Model energy landscapes and the force-induced dissociation of ligand-receptor bonds
    • Strunz, T., Oroszlan, K., Schumakovitch, I., Guntherodt, H. J. & Hegner, M. Model energy landscapes and the force-induced dissociation of ligand-receptor bonds. Biophys. J. 79, 1206-1212 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 1206-1212
    • Strunz, T.1    Oroszlan, K.2    Schumakovitch, I.3    Guntherodt, H.J.4    Hegner, M.5
  • 46
    • 44249115874 scopus 로고    scopus 로고
    • Self-assembled monolayers containing terminal mono-, bis-, and tris-nitrilotriacetic acid groups: Characterization and application
    • Valiokas, R. et al. Self-assembled monolayers containing terminal mono-, bis-, and tris-nitrilotriacetic acid groups: characterization and application. Langmuir 24, 4959-4967 (2008).
    • (2008) Langmuir , vol.24 , pp. 4959-4967
    • Valiokas, R.1
  • 47
    • 73249133401 scopus 로고    scopus 로고
    • Data analysis of translocation events in nanopore experiments
    • Pedone, D., Firnkes, M. & Rant, U. Data analysis of translocation events in nanopore experiments. Anal. Chem. 81, 9689-9694 (2009).
    • (2009) Anal. Chem. , vol.81 , pp. 9689-9694
    • Pedone, D.1    Firnkes, M.2    Rant, U.3
  • 48
    • 0036919576 scopus 로고    scopus 로고
    • Protein A is a virulence factor in Staphylococcus aureus arthritis and septic death
    • Palmqvist, N., Foster, T., Tarkowski, A. & Josefsson, E. Protein A is a virulence factor in Staphylococcus aureus arthritis and septic death. Microb. Pathog. 33, 239-249 (2002).
    • (2002) Microb. Pathog. , vol.33 , pp. 239-249
    • Palmqvist, N.1    Foster, T.2    Tarkowski, A.3    Josefsson, E.4
  • 49
    • 0020565892 scopus 로고
    • Binding of immunoglobulins to protein-A and immunoglobulin levels in mammalian sera
    • Lindmark, R., Thorentolling, K. & Sjoquist, J. Binding of immunoglobulins to protein-A and immunoglobulin levels in mammalian sera. J. Immunol. Methods 62, 1-13 (1983).
    • (1983) J. Immunol. Methods , vol.62 , pp. 1-13
    • Lindmark, R.1    Thorentolling, K.2    Sjoquist, J.3
  • 50
    • 0019468470 scopus 로고
    • Rat IgG subclasses: Differences in affinity to protein A-sepharose
    • Rousseaux, J., Picque, M. T., Bazin, H. & Biserte, G. Rat IgG subclasses: differences in affinity to protein A-sepharose. Mol. Immunol. 18, 639-645 (1981).
    • (1981) Mol. Immunol. , vol.18 , pp. 639-645
    • Rousseaux, J.1    Picque, M.T.2    Bazin, H.3    Biserte, G.4
  • 51
    • 0019994939 scopus 로고
    • Isolation of two immunoglobulin G subclasses, IgG2 and IgG1, from hamster serum using protein A-sepharose
    • Escribano, M. J., Haddada, H. & de Vaux Saint Cyr, C. Isolation of two immunoglobulin G subclasses, IgG2 and IgG1, from hamster serum using protein A-sepharose. J. Immunol. Methods 52, 63-72 (1982).
    • (1982) J. Immunol. Methods , vol.52 , pp. 63-72
    • Escribano, M.J.1    Haddada, H.2    De Vaux Saint Cyr, C.3
  • 52
    • 0017815498 scopus 로고
    • Humoral immunity and serum-proteins in syrian-hamster
    • Coe, J. E. Humoral immunity and serum-proteins in syrian-hamster. Fed. Proc. 37, 2030-2031 (1978).
    • (1978) Fed. Proc. , vol.37 , pp. 2030-2031
    • Coe, J.E.1


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