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Volumn 131, Issue 1, 2008, Pages 323-332

Optimisation of analyte transport in integrated microfluidic affinity sensors for the quantification of low levels of analyte

Author keywords

Affinity sensor; Analyte depletion; Biosensor; Design optimisation; Detection; Fluidic channel; Laminar flow; Mass transfer; Microfluidics; Recognition molecule

Indexed keywords

ANALYTIC EQUIPMENT; CHANNEL FLOW; LAMINAR FLOW; MASS TRANSFER; MICROFLUIDICS; OPTIMIZATION;

EID: 41449111116     PISSN: 09254005     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.snb.2007.11.034     Document Type: Article
Times cited : (17)

References (30)
  • 1
    • 34247097227 scopus 로고    scopus 로고
    • Biosensors as useful tools for environmental analysis and monitoring
    • Rodriguez-Mozaz S., de Alda M.J.L., and Barcelo D. Biosensors as useful tools for environmental analysis and monitoring. Anal. Bioanal. Chem. 386 4 (2006) 1025-1041
    • (2006) Anal. Bioanal. Chem. , vol.386 , Issue.4 , pp. 1025-1041
    • Rodriguez-Mozaz, S.1    de Alda, M.J.L.2    Barcelo, D.3
  • 3
    • 33845906055 scopus 로고    scopus 로고
    • Fluorescence sensing of intermolecular interactions and development of direct molecular biosensors
    • Altschuh D., Oncul S., and Demchenko A.P. Fluorescence sensing of intermolecular interactions and development of direct molecular biosensors. J. Mol. Recognit. 19 (2006) 459-477
    • (2006) J. Mol. Recognit. , vol.19 , pp. 459-477
    • Altschuh, D.1    Oncul, S.2    Demchenko, A.P.3
  • 4
    • 0032626631 scopus 로고    scopus 로고
    • Surface plasmon resonance sensors: review
    • Homola J., Yee S.S., and Gauglitz G. Surface plasmon resonance sensors: review. Sens. Actuators B 54 1-2 (1999) 3-15
    • (1999) Sens. Actuators B , vol.54 , Issue.1-2 , pp. 3-15
    • Homola, J.1    Yee, S.S.2    Gauglitz, G.3
  • 5
    • 23044506105 scopus 로고    scopus 로고
    • Kinetic determinations of molecular interactions using biacore-minimum data requirements for efficient experimental design
    • Önell A., and Andersson K. Kinetic determinations of molecular interactions using biacore-minimum data requirements for efficient experimental design. J. Mol. Recognit. 18 4 (2005) 307-317
    • (2005) J. Mol. Recognit. , vol.18 , Issue.4 , pp. 307-317
    • Önell, A.1    Andersson, K.2
  • 6
    • 0036022012 scopus 로고    scopus 로고
    • Transport and kinetic processes underlying biomolecular interactions in the biacore optical biosensor
    • Sikavitsas V., Nitsche J.M., and Mountziaris T.J. Transport and kinetic processes underlying biomolecular interactions in the biacore optical biosensor. Biotechnol. Prog. 18 4 (2002) 885-897
    • (2002) Biotechnol. Prog. , vol.18 , Issue.4 , pp. 885-897
    • Sikavitsas, V.1    Nitsche, J.M.2    Mountziaris, T.J.3
  • 7
    • 22344445940 scopus 로고    scopus 로고
    • Nanofluidics: what is it and what can we expect from it?
    • Eijkel J.C.T., and van den Berg A. Nanofluidics: what is it and what can we expect from it?. Microfluid. Nanofluid. 1 3 (2005) 249-267
    • (2005) Microfluid. Nanofluid. , vol.1 , Issue.3 , pp. 249-267
    • Eijkel, J.C.T.1    van den Berg, A.2
  • 8
    • 33746683073 scopus 로고    scopus 로고
    • Applications of antibody array platforms
    • Haab B.B. Applications of antibody array platforms. Curr. Opin. Biotechnol. 17 4 (2006) 415-421
    • (2006) Curr. Opin. Biotechnol. , vol.17 , Issue.4 , pp. 415-421
    • Haab, B.B.1
  • 9
    • 33747876481 scopus 로고    scopus 로고
    • Merging microfluidics with microarray-based bioassays
    • Situma C., Hashimoto M., and Soper S.A. Merging microfluidics with microarray-based bioassays. Biomol. Eng. 23 5 (2006) 213-231
    • (2006) Biomol. Eng. , vol.23 , Issue.5 , pp. 213-231
    • Situma, C.1    Hashimoto, M.2    Soper, S.A.3
  • 10
    • 23944527036 scopus 로고    scopus 로고
    • Single-molecule fluorescence detection in microfluidic channels-the holy grail in μTAS?
    • Dittrich P., and Manz A. Single-molecule fluorescence detection in microfluidic channels-the holy grail in μTAS?. Anal. Bioanal. Chem. 382 8 (2005) 1771-1782
    • (2005) Anal. Bioanal. Chem. , vol.382 , Issue.8 , pp. 1771-1782
    • Dittrich, P.1    Manz, A.2
  • 11
    • 29144495250 scopus 로고    scopus 로고
    • Optimizing integrated optical chips for label-free (bio-) chemical sensing
    • Kunz R.E., and Cottier K. Optimizing integrated optical chips for label-free (bio-) chemical sensing. Anal. Bioanal. Chem. 384 1 (2006) 180-190
    • (2006) Anal. Bioanal. Chem. , vol.384 , Issue.1 , pp. 180-190
    • Kunz, R.E.1    Cottier, K.2
  • 12
    • 0034318909 scopus 로고    scopus 로고
    • Formation of gradients of proteins on surfaces with microfluidic networks
    • Caelen I., Bernard A., Juncker D., Michel B., Heinzelmann H., and Delamarche E. Formation of gradients of proteins on surfaces with microfluidic networks. Langmuir 16 24 (2000) 9125-9130
    • (2000) Langmuir , vol.16 , Issue.24 , pp. 9125-9130
    • Caelen, I.1    Bernard, A.2    Juncker, D.3    Michel, B.4    Heinzelmann, H.5    Delamarche, E.6
  • 13
    • 0032752117 scopus 로고    scopus 로고
    • The influence of transport on the kinetics of binding to surface receptors: application to cells and biacore
    • Goldstein B., Coombs D., He X.Y., Pineda A.R., and Wofsy C. The influence of transport on the kinetics of binding to surface receptors: application to cells and biacore. J. Mol. Recognit. 12 5 (1999) 293-299
    • (1999) J. Mol. Recognit. , vol.12 , Issue.5 , pp. 293-299
    • Goldstein, B.1    Coombs, D.2    He, X.Y.3    Pineda, A.R.4    Wofsy, C.5
  • 15
    • 14544286392 scopus 로고    scopus 로고
    • Micromixers-a review on passive and active mixing principles
    • Hessel V., Lowe H., and Schonfeld F. Micromixers-a review on passive and active mixing principles. Chem. Eng. Sci. 60 8-9 (2005) 2479-2501
    • (2005) Chem. Eng. Sci. , vol.60 , Issue.8-9 , pp. 2479-2501
    • Hessel, V.1    Lowe, H.2    Schonfeld, F.3
  • 16
    • 0035387445 scopus 로고    scopus 로고
    • Adaptation of a surface plasmon resonance biosensor with miorofluidics for use with small sample volumes and long contact times
    • Abrantes M., Magone M.T., Boyd L.F., and Schuck P. Adaptation of a surface plasmon resonance biosensor with miorofluidics for use with small sample volumes and long contact times. Anal. Chem. 73 13 (2001) 2828-2835
    • (2001) Anal. Chem. , vol.73 , Issue.13 , pp. 2828-2835
    • Abrantes, M.1    Magone, M.T.2    Boyd, L.F.3    Schuck, P.4
  • 17
    • 0037418421 scopus 로고    scopus 로고
    • Evaluation of a three-dimensional micromixer in a surface-based biosensor
    • Vijayendran R.A., Motsegood K.M., Beebe D.J., and Leckband D.E. Evaluation of a three-dimensional micromixer in a surface-based biosensor. Langmuir 19 5 (2003) 1824-1828
    • (2003) Langmuir , vol.19 , Issue.5 , pp. 1824-1828
    • Vijayendran, R.A.1    Motsegood, K.M.2    Beebe, D.J.3    Leckband, D.E.4
  • 20
    • 1342264260 scopus 로고    scopus 로고
    • A novel nanolayer biosensor principle
    • Jennissen H.P., and Zumbrink T. A novel nanolayer biosensor principle. Biosens. Bioelectron. 19 9 (2004) 987-997
    • (2004) Biosens. Bioelectron. , vol.19 , Issue.9 , pp. 987-997
    • Jennissen, H.P.1    Zumbrink, T.2
  • 21
    • 29344451451 scopus 로고    scopus 로고
    • Mass transport and surface reactions in microfluidic systems
    • Gervais T., and Jensen K.F. Mass transport and surface reactions in microfluidic systems. Chem. Eng. Sci. 61 (2006) 1102-1121
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 1102-1121
    • Gervais, T.1    Jensen, K.F.2
  • 22
    • 0038616312 scopus 로고    scopus 로고
    • Surface plasmon field-enhanced fluorescence spectroscopy studies of the interaction between an antibody and its surface-coupled antigen
    • Yu F., Yao D.F., and Knoll W. Surface plasmon field-enhanced fluorescence spectroscopy studies of the interaction between an antibody and its surface-coupled antigen. Anal. Chem. 75 11 (2003) 2610-2617
    • (2003) Anal. Chem. , vol.75 , Issue.11 , pp. 2610-2617
    • Yu, F.1    Yao, D.F.2    Knoll, W.3
  • 23
    • 0031848098 scopus 로고    scopus 로고
    • Extending the range of rate constants available from biacore: interpreting mass transport-influenced binding data
    • Myszka D.G., He X., Dembo M., Morton T.A., and Goldstein B. Extending the range of rate constants available from biacore: interpreting mass transport-influenced binding data. Biophys. J. 75 2 (1998) 583-594
    • (1998) Biophys. J. , vol.75 , Issue.2 , pp. 583-594
    • Myszka, D.G.1    He, X.2    Dembo, M.3    Morton, T.A.4    Goldstein, B.5
  • 24
    • 24944498780 scopus 로고    scopus 로고
    • Microfluidics: fluid physics at the nanoliter scale
    • Squires T.M., and Quake S.R. Microfluidics: fluid physics at the nanoliter scale. Rev. Mod. Phys. 77 3 (2005) 977-1026
    • (2005) Rev. Mod. Phys. , vol.77 , Issue.3 , pp. 977-1026
    • Squires, T.M.1    Quake, S.R.2
  • 26
    • 0036218290 scopus 로고    scopus 로고
    • Effective rate models for receptors distributed in a layer above a surface: application to cells and biacore
    • Wofsy C., and Goldstein B. Effective rate models for receptors distributed in a layer above a surface: application to cells and biacore. Biophys. J. 82 4 (2002) 1743-1755
    • (2002) Biophys. J. , vol.82 , Issue.4 , pp. 1743-1755
    • Wofsy, C.1    Goldstein, B.2
  • 27
    • 0033254310 scopus 로고    scopus 로고
    • Transport effects on surface-volume biological reactions
    • Edwards D.A., Goldstein B., and Cohen D.S. Transport effects on surface-volume biological reactions. J. Math. Biol. 39 6 (1999) 533-561
    • (1999) J. Math. Biol. , vol.39 , Issue.6 , pp. 533-561
    • Edwards, D.A.1    Goldstein, B.2    Cohen, D.S.3
  • 28
    • 0027251108 scopus 로고
    • Rapid protein separation and diffusion-coefficient measurement by frit inlet flow field-flow fractionation
    • Liu M.K., Li P., and Giddings J.C. Rapid protein separation and diffusion-coefficient measurement by frit inlet flow field-flow fractionation. Protein Sci. 2 9 (1993) 1520-1531
    • (1993) Protein Sci. , vol.2 , Issue.9 , pp. 1520-1531
    • Liu, M.K.1    Li, P.2    Giddings, J.C.3
  • 29
    • 10744224338 scopus 로고    scopus 로고
    • Observation and characterization of the interaction between a single immunoglobulin binding domain of protein L and two equivalents of human kappa light chains
    • Housden N.G., Harrison S., Housden H.R., Thomas K.A., Beckingham J.A., Roberts S.E., Bottomley S.P., Graille M., Stura E., and Gore M.G. Observation and characterization of the interaction between a single immunoglobulin binding domain of protein L and two equivalents of human kappa light chains. J. Biol. Chem. 279 10 (2004) 9370-9378
    • (2004) J. Biol. Chem. , vol.279 , Issue.10 , pp. 9370-9378
    • Housden, N.G.1    Harrison, S.2    Housden, H.R.3    Thomas, K.A.4    Beckingham, J.A.5    Roberts, S.E.6    Bottomley, S.P.7    Graille, M.8    Stura, E.9    Gore, M.G.10
  • 30
    • 0031194188 scopus 로고    scopus 로고
    • Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation
    • Christensen L.L.H. Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation. Anal. Biochem. 249 2 (1997) 153-164
    • (1997) Anal. Biochem. , vol.249 , Issue.2 , pp. 153-164
    • Christensen, L.L.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.