메뉴 건너뛰기




Volumn 17, Issue 4, 2006, Pages 400-405

Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSENSORS; PROTEINS; REAL TIME SYSTEMS; SURFACE PLASMON RESONANCE;

EID: 33746742909     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2006.06.012     Document Type: Review
Times cited : (306)

References (40)
  • 2
    • 0035478125 scopus 로고    scopus 로고
    • Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition
    • McDonnell J.M. Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition. Curr Opin Chem Biol 5 (2001) 572-577
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 572-577
    • McDonnell, J.M.1
  • 4
    • 0034214017 scopus 로고    scopus 로고
    • Development and application of surface plasmon resonance-based biosensors for the detection of cell-ligand interactions
    • Quinn J.G., O'Neill S., Doyle A., McAtamney C., Diamond D., MacCraith B.D., and O'Kennedy R. Development and application of surface plasmon resonance-based biosensors for the detection of cell-ligand interactions. Anal Biochem 281 (2000) 135-143
    • (2000) Anal Biochem , vol.281 , pp. 135-143
    • Quinn, J.G.1    O'Neill, S.2    Doyle, A.3    McAtamney, C.4    Diamond, D.5    MacCraith, B.D.6    O'Kennedy, R.7
  • 5
    • 1842580880 scopus 로고    scopus 로고
    • Parallel, quantitative measurement of protein binding to a 120-element double-stranded DNA array in real time using surface plasmon resonance microscopy
    • Shumaker-Parry J.S., Aebersold R., and Campbell C.T. Parallel, quantitative measurement of protein binding to a 120-element double-stranded DNA array in real time using surface plasmon resonance microscopy. Anal Chem 76 (2004) 2071-2082
    • (2004) Anal Chem , vol.76 , pp. 2071-2082
    • Shumaker-Parry, J.S.1    Aebersold, R.2    Campbell, C.T.3
  • 6
    • 0032729972 scopus 로고    scopus 로고
    • Interaction of the human NF-kappa B p52 transcription factor with DNA-PNA hybrids mimicking the NF-kappa B binding sites of the human immunodeficiency virus type 1 promoter
    • Mischiati C., Borgatti M., Bianchi N., Rutigliano C., Tomassetti M., Feriotto G., and Gambari R. Interaction of the human NF-kappa B p52 transcription factor with DNA-PNA hybrids mimicking the NF-kappa B binding sites of the human immunodeficiency virus type 1 promoter. J Biol Chem 274 (1999) 33114-33122
    • (1999) J Biol Chem , vol.274 , pp. 33114-33122
    • Mischiati, C.1    Borgatti, M.2    Bianchi, N.3    Rutigliano, C.4    Tomassetti, M.5    Feriotto, G.6    Gambari, R.7
  • 7
    • 0030917801 scopus 로고    scopus 로고
    • Observation of hybridization and dehybridization of thiol-tethered DNA using two-color surface plasmon resonance spectroscopy
    • Peterlinz K.A., and Georgiadis R.M. Observation of hybridization and dehybridization of thiol-tethered DNA using two-color surface plasmon resonance spectroscopy. J Am Chem Soc 119 (1997) 3401-3402
    • (1997) J Am Chem Soc , vol.119 , pp. 3401-3402
    • Peterlinz, K.A.1    Georgiadis, R.M.2
  • 8
    • 0037065343 scopus 로고    scopus 로고
    • Hybridization of mismatched or partially matched DNA at surfaces
    • Peterson A.W., Wolf L.K., and Georgiadis R.M. Hybridization of mismatched or partially matched DNA at surfaces. J Am Chem Soc 124 (2002) 14601-14607
    • (2002) J Am Chem Soc , vol.124 , pp. 14601-14607
    • Peterson, A.W.1    Wolf, L.K.2    Georgiadis, R.M.3
  • 11
    • 3042757210 scopus 로고    scopus 로고
    • Self-assembling protein microarrays
    • This paper presents a novel method for preparing protein arrays directly from a cDNA chip via on-chip expression in a cell-free system. This approach eliminates the needs for protein purification and produces proteins at the time of use, which should reduce problems associated with storage and protein stability.
    • Ramachandran N., Hainsworth E., Bhullar B., Eisenstein S., Rosen B., Lau A.Y., Walter J.C., and LaBaer J. Self-assembling protein microarrays. Science 305 (2004) 86-90. This paper presents a novel method for preparing protein arrays directly from a cDNA chip via on-chip expression in a cell-free system. This approach eliminates the needs for protein purification and produces proteins at the time of use, which should reduce problems associated with storage and protein stability.
    • (2004) Science , vol.305 , pp. 86-90
    • Ramachandran, N.1    Hainsworth, E.2    Bhullar, B.3    Eisenstein, S.4    Rosen, B.5    Lau, A.Y.6    Walter, J.C.7    LaBaer, J.8
  • 12
    • 0037987418 scopus 로고
    • Surface-plasmon microscopy
    • Rothenhausler B., and Knoll W. Surface-plasmon microscopy. Nature 332 (1988) 615-617
    • (1988) Nature , vol.332 , pp. 615-617
    • Rothenhausler, B.1    Knoll, W.2
  • 13
    • 0023410221 scopus 로고
    • Surface-plasmon microscopy
    • Yeatman E., and Ash E.A. Surface-plasmon microscopy. Electron Lett 23 (1987) 1091-1092
    • (1987) Electron Lett , vol.23 , pp. 1091-1092
    • Yeatman, E.1    Ash, E.A.2
  • 14
    • 0033654653 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging measurements of ultrathin organic films
    • Brockman J.M., Nelson B.P., and Corn R.M. Surface plasmon resonance imaging measurements of ultrathin organic films. Annu Rev Phys Chem 51 (2000) 41-63
    • (2000) Annu Rev Phys Chem , vol.51 , pp. 41-63
    • Brockman, J.M.1    Nelson, B.P.2    Corn, R.M.3
  • 15
    • 1242293711 scopus 로고    scopus 로고
    • Quantitative methods for spatially resolved adsorption/desorption measurements in real time by surface plasmon resonance microscopy
    • Shumaker-Parry J.S., and Campbell C.T. Quantitative methods for spatially resolved adsorption/desorption measurements in real time by surface plasmon resonance microscopy. Anal Chem 76 (2004) 907-917
    • (2004) Anal Chem , vol.76 , pp. 907-917
    • Shumaker-Parry, J.S.1    Campbell, C.T.2
  • 16
    • 28544433116 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging measurements of the inhibition of Shiga-like toxin by synthetic multivalent inhibitors
    • Kanda V., Kitov P., Bundle D.R., and McDermott M.T. Surface plasmon resonance imaging measurements of the inhibition of Shiga-like toxin by synthetic multivalent inhibitors. Anal Chem 77 (2005) 7497-7504
    • (2005) Anal Chem , vol.77 , pp. 7497-7504
    • Kanda, V.1    Kitov, P.2    Bundle, D.R.3    McDermott, M.T.4
  • 17
    • 14244265717 scopus 로고    scopus 로고
    • Induced fit of an epitope peptide to a monoclonal antibody probed with a novel parallel surface plasmon resonance assay
    • Baggio R., Carven G.J., Chiulli A., Palmer M., Stern L.J., and Arenas J.E. Induced fit of an epitope peptide to a monoclonal antibody probed with a novel parallel surface plasmon resonance assay. J Biol Chem 280 (2005) 4188-4194
    • (2005) J Biol Chem , vol.280 , pp. 4188-4194
    • Baggio, R.1    Carven, G.J.2    Chiulli, A.3    Palmer, M.4    Stern, L.J.5    Arenas, J.E.6
  • 18
    • 20644438243 scopus 로고    scopus 로고
    • A novel approach to protein expression profiling using antibody microarrays combined with surface plasmon resonance technology
    • Usui-Aoki K., Shimada K., Nagano M., Kawai M., and Koga H. A novel approach to protein expression profiling using antibody microarrays combined with surface plasmon resonance technology. Proteomics 5 (2005) 2396-2401
    • (2005) Proteomics , vol.5 , pp. 2396-2401
    • Usui-Aoki, K.1    Shimada, K.2    Nagano, M.3    Kawai, M.4    Koga, H.5
  • 19
    • 0001743904 scopus 로고    scopus 로고
    • In situ surface plasmon resonance imaging detection of DNA hybridization to oligonucleotide arrays on gold surfaces
    • Thiel A.J., Frutos A.G., Jordan C.E., Corn R.M., and Smith L.M. In situ surface plasmon resonance imaging detection of DNA hybridization to oligonucleotide arrays on gold surfaces. Anal Chem 69 (1997) 4948-4956
    • (1997) Anal Chem , vol.69 , pp. 4948-4956
    • Thiel, A.J.1    Frutos, A.G.2    Jordan, C.E.3    Corn, R.M.4    Smith, L.M.5
  • 20
    • 29044433050 scopus 로고    scopus 로고
    • Quantitative angle-resolved SPR imaging of DNA-DNA and DNA-drug kinetics
    • Wolf L.K., Fullenkamp D.E., and Georgiadis R.M. Quantitative angle-resolved SPR imaging of DNA-DNA and DNA-drug kinetics. J Am Chem Soc 127 (2005) 17453-17459
    • (2005) J Am Chem Soc , vol.127 , pp. 17453-17459
    • Wolf, L.K.1    Fullenkamp, D.E.2    Georgiadis, R.M.3
  • 21
    • 10444221764 scopus 로고    scopus 로고
    • Analysis of mu-contact printed protein patterns by SPR imaging with a LED light source
    • Wilkop T., Wang Z.Z., and Cheng Q. Analysis of mu-contact printed protein patterns by SPR imaging with a LED light source. Langmuir 20 (2004) 11141-11148
    • (2004) Langmuir , vol.20 , pp. 11141-11148
    • Wilkop, T.1    Wang, Z.Z.2    Cheng, Q.3
  • 22
    • 27944501164 scopus 로고    scopus 로고
    • Label-free detection of proteins in crude cell lysate with antibody arrays by a surface plasmon resonance imaging technique
    • Kyo M., Usui-Aoki K., and Koga H. Label-free detection of proteins in crude cell lysate with antibody arrays by a surface plasmon resonance imaging technique. Anal Chem 77 (2005) 7115-7121
    • (2005) Anal Chem , vol.77 , pp. 7115-7121
    • Kyo, M.1    Usui-Aoki, K.2    Koga, H.3
  • 23
    • 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 (2003) 2610-2617
    • (2003) Anal Chem , vol.75 , pp. 2610-2617
    • Yu, F.1    Yao, D.F.2    Knoll, W.3
  • 24
    • 11244313892 scopus 로고    scopus 로고
    • Survey of the year 2003 commercial optical biosensor literature
    • Rich R.L., and Myszka D.G. Survey of the year 2003 commercial optical biosensor literature. J Mol Recognit 18 (2005) 1-39
    • (2005) J Mol Recognit , vol.18 , pp. 1-39
    • Rich, R.L.1    Myszka, D.G.2
  • 25
    • 27744519033 scopus 로고    scopus 로고
    • Survey of the year 2004 commercial optical biosensor literature
    • A very comprehensive review of the year's SPR literature, with valuable advice on experimental design and data analysis.
    • Rich R.L., and Myszka D.G. Survey of the year 2004 commercial optical biosensor literature. J Mol Recognit 18 (2005) 431-478. A very comprehensive review of the year's SPR literature, with valuable advice on experimental design and data analysis.
    • (2005) J Mol Recognit , vol.18 , pp. 431-478
    • Rich, R.L.1    Myszka, D.G.2
  • 26
    • 0842331880 scopus 로고    scopus 로고
    • A survey of the year 2002 commercial optical biosensor literature
    • Rich R.L., and Myszka D.G. A survey of the year 2002 commercial optical biosensor literature. J Mol Recognit 16 (2003) 351-382
    • (2003) J Mol Recognit , vol.16 , pp. 351-382
    • Rich, R.L.1    Myszka, D.G.2
  • 28
    • 0034426623 scopus 로고    scopus 로고
    • Application of surface plasmon resonance toward studies of low-molecular-weight antigen-antibody binding interactions
    • Adamczyk M., Moore J.A., and Yu Z.G. Application of surface plasmon resonance toward studies of low-molecular-weight antigen-antibody binding interactions. Methods - A Companion to Methods in Enzymology 20 (2000) 319-328
    • (2000) Methods - A Companion to Methods in Enzymology , vol.20 , pp. 319-328
    • Adamczyk, M.1    Moore, J.A.2    Yu, Z.G.3
  • 29
    • 0035884143 scopus 로고    scopus 로고
    • High-resolution and high-throughput protocols for measuring drug/human serum albumin interactions using BIACORE
    • Rich R.L., Day Y.S.N., Morton T.A., and Myszka D.G. High-resolution and high-throughput protocols for measuring drug/human serum albumin interactions using BIACORE. Anal Biochem 296 (2001) 197-207
    • (2001) Anal Biochem , vol.296 , pp. 197-207
    • Rich, R.L.1    Day, Y.S.N.2    Morton, T.A.3    Myszka, D.G.4
  • 31
    • 0034604110 scopus 로고    scopus 로고
    • Mechanisms of disease: role of transforming growth factor beta in human disease
    • Blobe G.C., Schiemann W.P., and Lodish H.F. Mechanisms of disease: role of transforming growth factor beta in human disease. N Engl J Med 342 (2000) 1350-1358
    • (2000) N Engl J Med , vol.342 , pp. 1350-1358
    • Blobe, G.C.1    Schiemann, W.P.2    Lodish, H.F.3
  • 33
    • 2942733360 scopus 로고    scopus 로고
    • Enhancement of the antagonistic potency of transforming growth factor-alpha receptor extracellular domains by coiled coil-induced homo- and heterodimerization
    • In this paper, the authors used a de novo-designed heterodimerizing coiled/coil system to induce dimerization of RII and RIII cell-surface receptors. They then utilized SPR to study how the dimerization affected binding of TGF-β. On the basis of the SPR data, the authors calculated kinetic constants to describe the interactions.
    • De Crescenzo G., Pham P.L., Durocher Y., Chao H., and O'Connor-McCourt MD. Enhancement of the antagonistic potency of transforming growth factor-alpha receptor extracellular domains by coiled coil-induced homo- and heterodimerization. J Biol Chem 279 (2004) 26013-26018. In this paper, the authors used a de novo-designed heterodimerizing coiled/coil system to induce dimerization of RII and RIII cell-surface receptors. They then utilized SPR to study how the dimerization affected binding of TGF-β. On the basis of the SPR data, the authors calculated kinetic constants to describe the interactions.
    • (2004) J Biol Chem , vol.279 , pp. 26013-26018
    • De Crescenzo, G.1    Pham, P.L.2    Durocher, Y.3    Chao, H.4    O'Connor-McCourt MD5
  • 34
    • 0242684423 scopus 로고    scopus 로고
    • Transforming growth factor-beta (TGF-β) binding to the extracellular domain of the type II TGF-β receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding
    • De Crescenzo G., Pham P.L., Durocher Y., and O'Connor-McCourt M.D. Transforming growth factor-beta (TGF-β) binding to the extracellular domain of the type II TGF-β receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding. J Mol Biol 328 (2003) 1173-1183
    • (2003) J Mol Biol , vol.328 , pp. 1173-1183
    • De Crescenzo, G.1    Pham, P.L.2    Durocher, Y.3    O'Connor-McCourt, M.D.4
  • 35
    • 0034724570 scopus 로고    scopus 로고
    • Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding
    • Herberg F.W., Maleszka A., Eide T., Vossebein L., and Tasken K. Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding. J Mol Biol 298 (2000) 329-339
    • (2000) J Mol Biol , vol.298 , pp. 329-339
    • Herberg, F.W.1    Maleszka, A.2    Eide, T.3    Vossebein, L.4    Tasken, K.5
  • 36
    • 0347359115 scopus 로고    scopus 로고
    • A BIAcore biosensor method for detailed kinetic binding analysis of small molecule inhibitors of p38 alpha mitogen-activated protein kinase
    • Casper D., Bukhtiyarova M., and Springman E.B. A BIAcore biosensor method for detailed kinetic binding analysis of small molecule inhibitors of p38 alpha mitogen-activated protein kinase. Anal Biochem 325 (2004) 126-136
    • (2004) Anal Biochem , vol.325 , pp. 126-136
    • Casper, D.1    Bukhtiyarova, M.2    Springman, E.B.3
  • 37
    • 17444407490 scopus 로고    scopus 로고
    • Kinetic studies of small molecule interactions with protein kinases using biosensor technology
    • Nordin H., Jungnelius M., Karlsson R., and Karlsson O.P. Kinetic studies of small molecule interactions with protein kinases using biosensor technology. Anal Biochem 340 (2005) 359-368
    • (2005) Anal Biochem , vol.340 , pp. 359-368
    • Nordin, H.1    Jungnelius, M.2    Karlsson, R.3    Karlsson, O.P.4
  • 38
    • 0035884115 scopus 로고    scopus 로고
    • Serological analysis of human anti-human antibody responses in colon cancer patients treated with repeated doses of humanized monoclonal antibody A33
    • Ritter G., Cohen L.S., Williams C., Richards E.C., Old L.J., and Welt S. Serological analysis of human anti-human antibody responses in colon cancer patients treated with repeated doses of humanized monoclonal antibody A33. Cancer Res 61 (2001) 6851-6859
    • (2001) Cancer Res , vol.61 , pp. 6851-6859
    • Ritter, G.1    Cohen, L.S.2    Williams, C.3    Richards, E.C.4    Old, L.J.5    Welt, S.6
  • 39
    • 0037107598 scopus 로고    scopus 로고
    • Surface plasmon resonance-based competition assay to assess the sera reactivity of variants of humanized antibodies
    • Gonzales N.R., Schuck P., Schlom J., and Kashmiri S.V.S. Surface plasmon resonance-based competition assay to assess the sera reactivity of variants of humanized antibodies. J Immunol Methods 268 (2002) 197-210
    • (2002) J Immunol Methods , vol.268 , pp. 197-210
    • Gonzales, N.R.1    Schuck, P.2    Schlom, J.3    Kashmiri, S.V.S.4
  • 40
    • 33645305964 scopus 로고    scopus 로고
    • High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays
    • In this paper, the authors developed an SPR-based array for screening a library of Fabs generated against human tissue kallikrein 1 (hK1), a serine protease linked to inflammation. Using the SPR array, the authors were able to measure kinetic constants for 96 unique Fabs simultaneously.
    • Wassaf D., Kuang G., Kopacz K., Wu Q.-L., Nguyen Q., Toews M., Cosic J., Jacques J., Wiltshire S., Lambert J., et al. High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays. Anal Biochem 351 (2006) 241-253. In this paper, the authors developed an SPR-based array for screening a library of Fabs generated against human tissue kallikrein 1 (hK1), a serine protease linked to inflammation. Using the SPR array, the authors were able to measure kinetic constants for 96 unique Fabs simultaneously.
    • (2006) Anal Biochem , vol.351 , pp. 241-253
    • Wassaf, D.1    Kuang, G.2    Kopacz, K.3    Wu, Q.-L.4    Nguyen, Q.5    Toews, M.6    Cosic, J.7    Jacques, J.8    Wiltshire, S.9    Lambert, J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.