메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages 401-407

Quantification of the affinities and kinetics of protein interactions using silicon nanowire biosensors

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; BINDING ENERGY; BIOSENSORS; KINETICS; LIGANDS; NANOWIRES; PROTEINS; RATE CONSTANTS; SILICON; SURFACE PLASMON RESONANCE;

EID: 84863720729     PISSN: 17483387     EISSN: 17483395     Source Type: Journal    
DOI: 10.1038/nnano.2012.82     Document Type: Article
Times cited : (329)

References (37)
  • 2
    • 18044367556 scopus 로고    scopus 로고
    • Biosensors for real-time in vivo measurements
    • Wilson, G. S. & Gifford, R. Biosensors for real-time in vivo measurements. Biosens. Bioelectron. 20, 2388-2403 (2005).
    • (2005) Biosens. Bioelectron. , vol.20 , pp. 2388-2403
    • Wilson, G.S.1    Gifford, R.2
  • 3
    • 32044456409 scopus 로고    scopus 로고
    • Nanotechnologies for biomolecular detection and medical diagnostics
    • Cheng, M. M. C. et al. Nanotechnologies for biomolecular detection and medical diagnostics. Curr. Opin. Chem. Biol. 10, 11-19 (2006).
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 11-19
    • Cheng, M.M.C.1
  • 4
    • 12444330291 scopus 로고    scopus 로고
    • Biosensors in clinical chemistry
    • D'Orazio, P. Biosensors in clinical chemistry. Clin. Chim. Acta 334, 41-69 (2003).
    • (2003) Clin. Chim. Acta , vol.334 , pp. 41-69
    • D'orazio, P.1
  • 5
    • 79955821190 scopus 로고    scopus 로고
    • Comparative advantages of mechanical biosensors
    • Arlett, J. L., Myers, E. B. & Roukes, M. L. Comparative advantages of mechanical biosensors. Nature Nanotech. 6, 203-215 (2011).
    • (2011) Nature Nanotech. , vol.6 , pp. 203-215
    • Arlett, J.L.1    Myers, E.B.2    Roukes, M.L.3
  • 6
    • 0036633640 scopus 로고    scopus 로고
    • Optical biosensors in drug discovery
    • Cooper, M. A. Optical biosensors in drug discovery. Nature Rev. Drug Discov. 1, 515-528 (2002).
    • (2002) Nature Rev. Drug Discov. , vol.1 , pp. 515-528
    • Cooper, M.A.1
  • 7
    • 58149218291 scopus 로고    scopus 로고
    • Real-time, label-free detection of biological entities using nanowire-based FETs
    • Curreli, M. et al. Real-time, label-free detection of biological entities using nanowire-based FETs. IEEE Trans. Nanotech. 7, 651-667 (2008).
    • (2008) IEEE Trans. Nanotech. , vol.7 , pp. 651-667
    • Curreli, M.1
  • 8
    • 56549085472 scopus 로고    scopus 로고
    • Semiconducting nanowire field-effect transistor biomolecular sensors
    • Stern, E., Vacic, A. & Reed, M. A. Semiconducting nanowire field-effect transistor biomolecular sensors. IEEE Trans. Electron Dev. 55, 3119-3130 (2008).
    • (2008) IEEE Trans. Electron Dev. , vol.55 , pp. 3119-3130
    • Stern, E.1    Vacic, A.2    Reed, M.A.3
  • 9
    • 0035793378 scopus 로고    scopus 로고
    • Functional nanoscale electronic devices assembled using silicon nanowire building blocks
    • Cui, Y. & Lieber, C. M. Functional nanoscale electronic devices assembled using silicon nanowire building blocks. Science 291, 851-853 (2001).
    • (2001) Science , vol.291 , pp. 851-853
    • Cui, Y.1    Lieber, C.M.2
  • 10
    • 33846695595 scopus 로고    scopus 로고
    • Label-free immunodetection with CMOS-compatible semiconducting nanowires
    • Stern, E. et al. Label-free immunodetection with CMOS-compatible semiconducting nanowires. Nature 445, 519-522 (2007).
    • (2007) Nature , vol.445 , pp. 519-522
    • Stern, E.1
  • 11
    • 14744276690 scopus 로고    scopus 로고
    • Label-free detection of small-molecule-protein interactions by using nanowire nanosensors
    • Wang, W. U., Chen, C., Lin, K. H., Fang, Y. & Lieber, C. M. Label-free detection of small-molecule-protein interactions by using nanowire nanosensors. Proc. Natl Acad. Sci. USA 102, 3208-3212 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3208-3212
    • Wang, W.U.1    Chen, C.2    Lin, K.H.3    Fang, Y.4    Lieber, C.M.5
  • 12
    • 79951646370 scopus 로고    scopus 로고
    • Quantifying signal changes in nano-wire based biosensors
    • De Vico, L. et al. Quantifying signal changes in nano-wire based biosensors. Nanoscale 3, 706-717 (2011).
    • (2011) Nanoscale , vol.3 , pp. 706-717
    • De Vico, L.1
  • 13
    • 33845595605 scopus 로고    scopus 로고
    • Quantitative real-time measurements of DNA hybridization with alkylated nonoxidized silicon nanowires in electrolyte solution
    • Bunimovich, Y. L. et al. Quantitative real-time measurements of DNA hybridization with alkylated nonoxidized silicon nanowires in electrolyte solution. J. Am. Chem. Soc. 128, 16323-16331 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16323-16331
    • Bunimovich, Y.L.1
  • 14
    • 41849151140 scopus 로고    scopus 로고
    • Making it stick: Convection, reaction and diffusion in surface-based biosensors
    • Squires, T. M., Messinger, R. J. & Manalis, S. R. Making it stick: convection, reaction and diffusion in surface-based biosensors. Nature Biotechnol. 26, 417-426 (2008).
    • (2008) Nature Biotechnol. , vol.26 , pp. 417-426
    • Squires, T.M.1    Messinger, R.J.2    Manalis, S.R.3
  • 15
    • 34247236200 scopus 로고    scopus 로고
    • Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE
    • Tian, J. et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nature Immunol. 8, 487-496 (2007).
    • (2007) Nature Immunol. , vol.8 , pp. 487-496
    • Tian, J.1
  • 16
    • 84863129261 scopus 로고    scopus 로고
    • DNA binding to proteolytically activated TLR9 is sequence-independent and enhanced by DNA curvature
    • Li, Y., Berk, I. C. & Modis, Y. DNA binding to proteolytically activated TLR9 is sequence-independent and enhanced by DNA curvature. EMBO J. 31, 919-931 (2012).
    • (2012) EMBO J. , vol.31 , pp. 919-931
    • Li, Y.1    Berk, I.C.2    Modis, Y.3
  • 17
    • 0025281379 scopus 로고
    • Introduction to avidin-biotin technology
    • Wilchek, M. & Bayer, E. A. Introduction to avidin-biotin technology. Methods Enzymol. 184, 5-13 (1990).
    • (1990) Methods Enzymol. , vol.184 , pp. 5-13
    • Wilchek, M.1    Bayer, E.A.2
  • 18
    • 78649726253 scopus 로고    scopus 로고
    • Challenges in the use of 1D nanostructures for on-chip biosensing and diagnostics: A review
    • Balasubramanian, K. Challenges in the use of 1D nanostructures for on-chip biosensing and diagnostics: a review. Biosens. Bioelectron. 26, 1195-1204 (2011).
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 1195-1204
    • Balasubramanian, K.1
  • 19
    • 73849132160 scopus 로고    scopus 로고
    • A calibration method for nanowire biosensors to suppress device-to-device variation
    • Ishikawa, F. N. et al. A calibration method for nanowire biosensors to suppress device-to-device variation. ACS Nano 3, 3969-3976 (2009).
    • (2009) ACS Nano , vol.3 , pp. 3969-3976
    • Ishikawa, F.N.1
  • 20
    • 79959795059 scopus 로고    scopus 로고
    • Universal parameters for carbon nanotube network-based sensors: Can nanotube sensors be reproducible?
    • Lee, B. Y. et al. Universal parameters for carbon nanotube network-based sensors: can nanotube sensors be reproducible? ACS Nano 5, 4373-4379 (2011).
    • (2011) ACS Nano , vol.5 , pp. 4373-4379
    • Lee, B.Y.1
  • 21
    • 34547381485 scopus 로고    scopus 로고
    • Quantitative detection of protein using a top-gate carbon nanotube field effect transistor
    • Abe, M. et al. Quantitative detection of protein using a top-gate carbon nanotube field effect transistor. J. Phys. Chem. C 111, 8667-8670 (2007).
    • (2007) J. Phys. Chem. C , vol.111 , pp. 8667-8670
    • Abe, M.1
  • 22
    • 0031848098 scopus 로고    scopus 로고
    • Extending the range of rate constants available from BIACORE: Interpreting mass transportinfluenced binding data
    • Myszka, D. G., He, X., Dembo, M., Morton, T. A. & Goldstein, B. Extending the range of rate constants available from BIACORE: interpreting mass transportinfluenced binding data. Biophys. J. 75, 583-594 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 583-594
    • Myszka, D.G.1    He, X.2    Dembo, M.3    Morton, T.A.4    Goldstein, B.5
  • 23
    • 79955870892 scopus 로고    scopus 로고
    • Quantification of protein interactions and solution transport using high-density GMR sensor arrays
    • Gaster, R. S. et al. Quantification of protein interactions and solution transport using high-density GMR sensor arrays. Nature Nanotech. 6, 314-320 (2011).
    • (2011) Nature Nanotech. , vol.6 , pp. 314-320
    • Gaster, R.S.1
  • 24
    • 43149112560 scopus 로고    scopus 로고
    • Silicon nanoribbons for electrical detection of biomolecules
    • Elfstroem, N., Karlstroem, A. E. & Linnrost, J. Silicon nanoribbons for electrical detection of biomolecules. Nano Lett. 8, 945-949 (2008).
    • (2008) Nano Lett. , vol.8 , pp. 945-949
    • Elfstroem, N.1    Karlstroem, A.E.2    Linnrost, J.3
  • 25
    • 18144396893 scopus 로고    scopus 로고
    • Detection limits for nanoscale biosensors
    • Sheehan, P. E. & Whitman, L. J. Detection limits for nanoscale biosensors. Nano Lett. 5, 803-807 (2005).
    • (2005) Nano Lett. , vol.5 , pp. 803-807
    • Sheehan, P.E.1    Whitman, L.J.2
  • 26
    • 0026034882 scopus 로고
    • A critical-evaluation of direct electrical protein-detection methods
    • Bergveld, P. A critical-evaluation of direct electrical protein-detection methods. Biosens. Bioelectron. 6, 55-72 (1991).
    • (1991) Biosens. Bioelectron. , vol.6 , pp. 55-72
    • Bergveld, P.1
  • 27
    • 36748999383 scopus 로고    scopus 로고
    • Importance of the debye screening length on nanowire field effect transistor sensors
    • Stern, E. et al. Importance of the debye screening length on nanowire field effect transistor sensors. Nano Lett. 7, 3405-3409 (2007).
    • (2007) Nano Lett. , vol.7 , pp. 3405-3409
    • Stern, E.1
  • 28
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear-protein HMG1
    • Bianchi, M. E., Beltrame, M. & Paonessa, G. Specific recognition of cruciform DNA by nuclear-protein HMG1. Science 243, 1056-1059 (1989).
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 29
    • 34250837518 scopus 로고    scopus 로고
    • A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA
    • Ivanov, S. et al. A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA. Blood 110, 1970-1981 (2007).
    • (2007) Blood , vol.110 , pp. 1970-1981
    • Ivanov, S.1
  • 30
    • 0033578010 scopus 로고    scopus 로고
    • Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins
    • Ohndorf, U. M., Rould, M. A., He, Q., Pabo, C. O. & Lippard, S. J. Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature 399, 708-712 (1999).
    • (1999) Nature , vol.399 , pp. 708-712
    • Ohndorf, U.M.1    Rould, M.A.2    He, Q.3    Pabo, C.O.4    Lippard, S.J.5
  • 31
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein-HMG1 to DNA damaged by the anticancer drug cisplatin
    • Pil, P. M. & Lippard, S. J. Specific binding of chromosomal protein-HMG1 to DNA damaged by the anticancer drug cisplatin. Science 256, 234-237 (1992).
    • (1992) Science , vol.256 , pp. 234-237
    • Pil, P.M.1    Lippard, S.J.2
  • 32
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • Halford, S. E. & Marko, J. F. How do site-specific DNA-binding proteins find their targets? Nucleic Acids Res. 32, 3040-3052 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 33
    • 0037432325 scopus 로고    scopus 로고
    • Nature of full-length HMGB1 binding to cisplatinmodified DNA
    • Jung, Y. & Lippard, S. J. Nature of full-length HMGB1 binding to cisplatinmodified DNA. Biochemistry 42, 2664-2671 (2003).
    • (2003) Biochemistry , vol.42 , pp. 2664-2671
    • Jung, Y.1    Lippard, S.J.2
  • 34
    • 0033554016 scopus 로고    scopus 로고
    • Molecular recognition between genetically engineered streptavidin and surface-bound biotin
    • Perez-Luna, V. H. et al. Molecular recognition between genetically engineered streptavidin and surface-bound biotin. J. Am. Chem. Soc. 121, 6469-6478 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6469-6478
    • Perez-Luna, V.H.1
  • 35
    • 0034316984 scopus 로고    scopus 로고
    • Binding and dissociation kinetics of wild-type and mutant streptavidins on mixed biotincontaining alkylthiolate monolayers
    • Jung, L. S., Nelson, K. E., Stayton, P. S. & Campbell, C. T. Binding and dissociation kinetics of wild-type and mutant streptavidins on mixed biotincontaining alkylthiolate monolayers. Langmuir 16, 9421-9432 (2000).
    • (2000) Langmuir , vol.16 , pp. 9421-9432
    • Jung, L.S.1    Nelson, K.E.2    Stayton, P.S.3    Campbell, C.T.4
  • 36
    • 0000652708 scopus 로고    scopus 로고
    • Ligand receptor dynamics at streptavidin-coated particle surfaces: A flow cytometric and spectrofluorimetric study
    • Buranda, T. et al. Ligand receptor dynamics at streptavidin-coated particle surfaces: a flow cytometric and spectrofluorimetric study. J. Phys. Chem. B 103, 3399-3410 (1999).
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3399-3410
    • Buranda, T.1
  • 37
    • 33645235292 scopus 로고    scopus 로고
    • Nonregeneration protocol for surface plasmon resonance: Study of high-affinity interaction with high-density biosensors
    • Tang, Y. J., Mernaugh, R. & Zeng, X. Q. Nonregeneration protocol for surface plasmon resonance: study of high-affinity interaction with high-density biosensors. Anal. Chem. 78, 1841-1848 (2006).
    • (2006) Anal. Chem. , vol.78 , pp. 1841-1848
    • Tang, Y.J.1    Mernaugh, R.2    Zeng, X.Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.