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Volumn 385, Issue 2, 2009, Pages 358-364

Metal-enhanced fluorescence of tryptophan residues in proteins: Application toward label-free bioassays

Author keywords

Intrinsic fluorescence of proteins; Label free detection; Localized surface plasmon resonance; Metal enhanced fluorescence

Indexed keywords

AMINO ACIDS; FLUORESCENCE; METAL NANOPARTICLES; PROTEINS; SILVER NANOPARTICLES; SURFACE PLASMON RESONANCE;

EID: 58149469495     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.11.025     Document Type: Article
Times cited : (73)

References (44)
  • 1
    • 33750595486 scopus 로고    scopus 로고
    • Label-free detection methods for protein microarrays
    • Yu X., Xu D., and Cheng Q. Label-free detection methods for protein microarrays. Proteomics 6 (2006) 5493-5503
    • (2006) Proteomics , vol.6 , pp. 5493-5503
    • Yu, X.1    Xu, D.2    Cheng, Q.3
  • 2
    • 33751218906 scopus 로고    scopus 로고
    • Non-optical screening platforms: the next wave in label-free screening?
    • Cooper M.A. Non-optical screening platforms: the next wave in label-free screening?. Drug Discov. Today 11 (2006) 1068-1074
    • (2006) Drug Discov. Today , vol.11 , pp. 1068-1074
    • Cooper, M.A.1
  • 3
    • 34250216703 scopus 로고    scopus 로고
    • Surface-enhanced Raman scattering based nonfluorescent probe for multiplex DNA detection
    • Sun L., Yu C., and Irudayaraj J. Surface-enhanced Raman scattering based nonfluorescent probe for multiplex DNA detection. Anal. Chem. 79 (2007) 3981-3988
    • (2007) Anal. Chem. , vol.79 , pp. 3981-3988
    • Sun, L.1    Yu, C.2    Irudayaraj, J.3
  • 4
    • 0037401054 scopus 로고    scopus 로고
    • New biochip technology for label-free detection of pathogens and their toxins
    • Grow A.E., Wood L.L., Chaycomb J.L., and Thompson P.A. New biochip technology for label-free detection of pathogens and their toxins. J. Microbiol. Methods 53 (2003) 221-233
    • (2003) J. Microbiol. Methods , vol.53 , pp. 221-233
    • Grow, A.E.1    Wood, L.L.2    Chaycomb, J.L.3    Thompson, P.A.4
  • 5
    • 39749124167 scopus 로고    scopus 로고
    • An overview of label-free electrochemical protein sensors
    • Vestergaard M., Kerman K., and Tamiya E. An overview of label-free electrochemical protein sensors. Sensors 7 (2007) 3442-3458
    • (2007) Sensors , vol.7 , pp. 3442-3458
    • Vestergaard, M.1    Kerman, K.2    Tamiya, E.3
  • 6
  • 7
    • 34248663217 scopus 로고    scopus 로고
    • Fabrication of silicon nanowire devices for ultrasensitive, label-free, real-time detection of biological and chemical species
    • Patolsky F., Zheng G., Lieber C.M., and ultrasensitive F.o.s.n.d.f. label-free real-time detection of biological and chemical species. Nat. Protocols 1 (2006) 1711-1724
    • (2006) Nat. Protocols , vol.1 , pp. 1711-1724
    • Patolsky, F.1    Zheng, G.2    Lieber, C.M.3
  • 8
  • 9
    • 33645460182 scopus 로고    scopus 로고
    • An optical biosensor for rapid and label-free detection of cells
    • Acharya G., Chang C.-L., and Savran C. An optical biosensor for rapid and label-free detection of cells. J. Am. Chem. Soc. 128 (2006) 3862-3863
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3862-3863
    • Acharya, G.1    Chang, C.-L.2    Savran, C.3
  • 11
    • 1642619447 scopus 로고    scopus 로고
    • Label-free detection of microarrays of biomolecules by oblique-incidence reflectivity difference microscopy
    • Landry J.P., Zhu X.D., and Gregg J.P. Label-free detection of microarrays of biomolecules by oblique-incidence reflectivity difference microscopy. Optics Lett. 29 (2004) 581-583
    • (2004) Optics Lett. , vol.29 , pp. 581-583
    • Landry, J.P.1    Zhu, X.D.2    Gregg, J.P.3
  • 13
    • 34250701133 scopus 로고    scopus 로고
    • Combined enhanced fluorescence and label-free biomolecular detection with a photonic crystal surface
    • Mathias P.C., Ganesh N., Chan L.L., and Cunningham B.T. Combined enhanced fluorescence and label-free biomolecular detection with a photonic crystal surface. Appl. Optics 46 (2007) 2351-2360
    • (2007) Appl. Optics , vol.46 , pp. 2351-2360
    • Mathias, P.C.1    Ganesh, N.2    Chan, L.L.3    Cunningham, B.T.4
  • 14
    • 33847230590 scopus 로고    scopus 로고
    • Recent advances in surface plasmon resonance based techniques for bioanalysis
    • Phillips K.S., and Cheng Q. Recent advances in surface plasmon resonance based techniques for bioanalysis. Anal. Bioanal. Chem. 387 (2007) 1831-1840
    • (2007) Anal. Bioanal. Chem. , vol.387 , pp. 1831-1840
    • Phillips, K.S.1    Cheng, Q.2
  • 15
    • 4744363460 scopus 로고    scopus 로고
    • Real-time surface plasmon resonance imaging measurements for the multiplexed determination of protein adsorption/desorption kinetics and surface enzymatic reactions on peptide microarrays
    • Wegner G.J., Wark A.W., Lee H.J., Codner E., Saeki T., Fang S., and Corn R.M. Real-time surface plasmon resonance imaging measurements for the multiplexed determination of protein adsorption/desorption kinetics and surface enzymatic reactions on peptide microarrays. Anal. Chem. 76 (2004) 5677-5684
    • (2004) Anal. Chem. , vol.76 , pp. 5677-5684
    • Wegner, G.J.1    Wark, A.W.2    Lee, H.J.3    Codner, E.4    Saeki, T.5    Fang, S.6    Corn, R.M.7
  • 16
    • 33748804979 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers
    • Lee H.J., Nedelkov D., and Corn R.M. Surface plasmon resonance imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers. Anal. Chem. 78 (2006) 6504-6510
    • (2006) Anal. Chem. , vol.78 , pp. 6504-6510
    • Lee, H.J.1    Nedelkov, D.2    Corn, R.M.3
  • 17
    • 0032162964 scopus 로고    scopus 로고
    • Quantitative interpretation of the response of surface plasmon resonance sensors to adsorbed films
    • Jung L.S., Campbell C.T., Chinowsky T.M., Mar M.N., and Yee S.S. Quantitative interpretation of the response of surface plasmon resonance sensors to adsorbed films. Langmuir 14 (1998) 5636-5648
    • (1998) Langmuir , vol.14 , pp. 5636-5648
    • Jung, L.S.1    Campbell, C.T.2    Chinowsky, T.M.3    Mar, M.N.4    Yee, S.S.5
  • 18
    • 0032626631 scopus 로고    scopus 로고
    • Surface plasmon resonance sensors: review
    • Homola J., Yee S.S., and Gauglitz G. Surface plasmon resonance sensors: review. Sens. Actuat. B 54 (1999) 3-15
    • (1999) Sens. Actuat. B , vol.54 , pp. 3-15
    • Homola, J.1    Yee, S.S.2    Gauglitz, G.3
  • 19
    • 4444246467 scopus 로고    scopus 로고
    • Biological sensing using transmission surface plasmon resonance spectroscopy
    • Lahav M., Vaskevich A., and Rubinstein I. Biological sensing using transmission surface plasmon resonance spectroscopy. Langmuir 20 (2004) 7365-7367
    • (2004) Langmuir , vol.20 , pp. 7365-7367
    • Lahav, M.1    Vaskevich, A.2    Rubinstein, I.3
  • 20
    • 0037019549 scopus 로고    scopus 로고
    • A nanoscale optical biosensor: sensitivity and selectivity of an approach based on the localized surface plasmon resonance spectroscopy of triangular silver nanoparticles
    • Haes A.J., and Van Duyne R.P. A nanoscale optical biosensor: sensitivity and selectivity of an approach based on the localized surface plasmon resonance spectroscopy of triangular silver nanoparticles. J. Am. Chem. Soc. 124 (2002) 10596-10604
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10596-10604
    • Haes, A.J.1    Van Duyne, R.P.2
  • 21
    • 0037468429 scopus 로고    scopus 로고
    • A nanoscale optical biosensor: real-time immunoassay in physiological buffer enabled by improved nanoparticle adhesion
    • Riboh J.C., Haes A.J., McFarland A.D., Yonzon C.R., and Van Duyne R.P. A nanoscale optical biosensor: real-time immunoassay in physiological buffer enabled by improved nanoparticle adhesion. J. Phys. Chem. B 107 (2003) 1772-1780
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1772-1780
    • Riboh, J.C.1    Haes, A.J.2    McFarland, A.D.3    Yonzon, C.R.4    Van Duyne, R.P.5
  • 23
    • 0346525122 scopus 로고    scopus 로고
    • Ultrasensitive detection of unstained proteins in acrylamide gels by native UV fluorescence
    • Roegener J., Lutter P., Reinhardt R., Blüggel M., Meyer H.E., and Anselmetti D. Ultrasensitive detection of unstained proteins in acrylamide gels by native UV fluorescence. Anal. Chem. 75 (2003) 157-159
    • (2003) Anal. Chem. , vol.75 , pp. 157-159
    • Roegener, J.1    Lutter, P.2    Reinhardt, R.3    Blüggel, M.4    Meyer, H.E.5    Anselmetti, D.6
  • 24
    • 1442324450 scopus 로고    scopus 로고
    • One- and two-dimensional miniaturized electrophoresis of proteins with native fluorescence detection
    • Sluszny C., and Yeung E.S. One- and two-dimensional miniaturized electrophoresis of proteins with native fluorescence detection. Anal. Chem. 76 (2004) 1359-1365
    • (2004) Anal. Chem. , vol.76 , pp. 1359-1365
    • Sluszny, C.1    Yeung, E.S.2
  • 25
    • 14744269750 scopus 로고    scopus 로고
    • Deep UV laser-induced fluorescence detection of unlabeled drugs and proteins in microchip electrophoresis
    • Schulze P., Ludwig M., Kohler F., and Belder D. Deep UV laser-induced fluorescence detection of unlabeled drugs and proteins in microchip electrophoresis. Anal. Chem. 77 (2005) 1325-1329
    • (2005) Anal. Chem. , vol.77 , pp. 1325-1329
    • Schulze, P.1    Ludwig, M.2    Kohler, F.3    Belder, D.4
  • 26
    • 32444435455 scopus 로고    scopus 로고
    • UV fluorescence lifetime imaging microscopy: a label-free method for detection and quantification of protein interactions
    • Schüttpeltz M., Müller C., Neuweiler H., and Sauer M. UV fluorescence lifetime imaging microscopy: a label-free method for detection and quantification of protein interactions. Anal. Chem. 78 (2006) 663-669
    • (2006) Anal. Chem. , vol.78 , pp. 663-669
    • Schüttpeltz, M.1    Müller, C.2    Neuweiler, H.3    Sauer, M.4
  • 27
    • 33748791493 scopus 로고    scopus 로고
    • A label-free continuous total-internal-reflection-fluorescence-based immunosensor
    • Engström H.A., Andersson P.O., and Ohlson S. A label-free continuous total-internal-reflection-fluorescence-based immunosensor. Anal. Biochem. 357 (2006) 159-166
    • (2006) Anal. Biochem. , vol.357 , pp. 159-166
    • Engström, H.A.1    Andersson, P.O.2    Ohlson, S.3
  • 28
    • 0035498894 scopus 로고    scopus 로고
    • Radiative decay engineering: biophysical and biomedical applications
    • Lakowicz J.R. Radiative decay engineering: biophysical and biomedical applications. Anal. Biochem. 298 (2001) 1-24
    • (2001) Anal. Biochem. , vol.298 , pp. 1-24
    • Lakowicz, J.R.1
  • 29
    • 0037083537 scopus 로고    scopus 로고
    • Radiative decay engineering: II. effects of silver island films on fluorescence intensity, lifetimes, and resonance energy transfer
    • Lakowicz J.R., Shen Y., D'Auria S., Malicka J., Fang J., Gryczynski Z., and Gryczynski I. Radiative decay engineering: II. effects of silver island films on fluorescence intensity, lifetimes, and resonance energy transfer. Anal. Biochem. 301 (2002) 261-277
    • (2002) Anal. Biochem. , vol.301 , pp. 261-277
    • Lakowicz, J.R.1    Shen, Y.2    D'Auria, S.3    Malicka, J.4    Fang, J.5    Gryczynski, Z.6    Gryczynski, I.7
  • 33
    • 34548550480 scopus 로고    scopus 로고
    • Aluminum nanostructured films as substrates for enhanced fluorescence in the ultraviolet-blue spectral region
    • Ray K., Chowdhury M.H., and Lakowicz J.R. Aluminum nanostructured films as substrates for enhanced fluorescence in the ultraviolet-blue spectral region. Anal. Chem. 79 (2007) 6480-6487
    • (2007) Anal. Chem. , vol.79 , pp. 6480-6487
    • Ray, K.1    Chowdhury, M.H.2    Lakowicz, J.R.3
  • 34
    • 59849118652 scopus 로고    scopus 로고
    • C. Sun, X. Wu, H. Ding, L. Zhao, F. Wang, J. Yang, X. Liu, The fluorescence enhancement of the protein adsorbed on the surface of Ag nanoparticle, J. Fluoresc. 10.1007/s10895-008-0392-4.
    • C. Sun, X. Wu, H. Ding, L. Zhao, F. Wang, J. Yang, X. Liu, The fluorescence enhancement of the protein adsorbed on the surface of Ag nanoparticle, J. Fluoresc. 10.1007/s10895-008-0392-4.
  • 35
    • 0022963068 scopus 로고
    • Chemical procedure for preparing surface-enhanced Raman scattering active silver films
    • Ni F., and Cotton T.M. Chemical procedure for preparing surface-enhanced Raman scattering active silver films. Anal. Chem. 58 (1986) 3159-3163
    • (1986) Anal. Chem. , vol.58 , pp. 3159-3163
    • Ni, F.1    Cotton, T.M.2
  • 36
    • 0037061949 scopus 로고    scopus 로고
    • Effect of the solvent refractive index on the excited-state lifetime of a single tryptophan residue in a protein
    • Toptygin D., Savtchenko R.S., Meadow N.D., Roseman S., and Brand L. Effect of the solvent refractive index on the excited-state lifetime of a single tryptophan residue in a protein. J. Phys. Chem. B 106 (2002) 3724-3734
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3724-3734
    • Toptygin, D.1    Savtchenko, R.S.2    Meadow, N.D.3    Roseman, S.4    Brand, L.5
  • 37
    • 0026011793 scopus 로고
    • Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules
    • Darst S.A., Ahlers M., Meller P.H., Kubalek E.W., Blakenburg R., Rib H.O., Ringsdorf H., and Kornberg R.D. Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules. Biophys. J. 59 (1991) 387-396
    • (1991) Biophys. J. , vol.59 , pp. 387-396
    • Darst, S.A.1    Ahlers, M.2    Meller, P.H.3    Kubalek, E.W.4    Blakenburg, R.5    Rib, H.O.6    Ringsdorf, H.7    Kornberg, R.D.8
  • 38
    • 54849440861 scopus 로고    scopus 로고
    • Field enhancement around metal nanoparticles and nanoshells: a systematic investigation
    • Tanabe K. Field enhancement around metal nanoparticles and nanoshells: a systematic investigation. J. Phys. Chem. C 112 (2008) 15721-15728
    • (2008) J. Phys. Chem. C , vol.112 , pp. 15721-15728
    • Tanabe, K.1
  • 39
    • 34648823390 scopus 로고    scopus 로고
    • Plasmon-enhanced luminescence near noble-metal nanospheres: comparison of exact theory and an improved Gersten and Nitzan model
    • Mertens H., Koendrink A.F., and Polman A. Plasmon-enhanced luminescence near noble-metal nanospheres: comparison of exact theory and an improved Gersten and Nitzan model. Phys. Rev. B 76 (2007) 115123
    • (2007) Phys. Rev. B , vol.76 , pp. 115123
    • Mertens, H.1    Koendrink, A.F.2    Polman, A.3
  • 40
    • 0000920873 scopus 로고    scopus 로고
    • Layer-by-layer deposition of avidin and biotin labeled antibody on a solid surface to prepare a multilayer array of antibody
    • Hoshi T., Saiki H., and Anzai J. Layer-by-layer deposition of avidin and biotin labeled antibody on a solid surface to prepare a multilayer array of antibody. J. Chem. Soc. Perkin Trans. 2 (1999) 1293-1294
    • (1999) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1293-1294
    • Hoshi, T.1    Saiki, H.2    Anzai, J.3
  • 41
    • 0034316984 scopus 로고    scopus 로고
    • Binding and dissociation kinetics of wild-type and mutant streptavidins on mixed biotin-containing alkylthiolate monolayers
    • Jung L.S., Nelson K.E., Stayton P.S., and Campbell C.T. Binding and dissociation kinetics of wild-type and mutant streptavidins on mixed biotin-containing alkylthiolate monolayers. Langmuir 16 (2000) 9421-9432
    • (2000) Langmuir , vol.16 , pp. 9421-9432
    • Jung, L.S.1    Nelson, K.E.2    Stayton, P.S.3    Campbell, C.T.4
  • 42
    • 4544227682 scopus 로고    scopus 로고
    • Label-free biosensing by surface plasmon resonance of nanoparticles on glass: optimization of nanoparticle size
    • Nath N., and Chilkoti A. Label-free biosensing by surface plasmon resonance of nanoparticles on glass: optimization of nanoparticle size. Anal. Chem. 76 (2004) 5370-5378
    • (2004) Anal. Chem. , vol.76 , pp. 5370-5378
    • Nath, N.1    Chilkoti, A.2
  • 43
    • 0030777594 scopus 로고    scopus 로고
    • SPR studies of nonspecific adsorption kinetics of human IgG and BSA on gold surfaces modified by self-assembled monolayers (SAMs)
    • Silin V., Weetall H., and Vanderah D.J. SPR studies of nonspecific adsorption kinetics of human IgG and BSA on gold surfaces modified by self-assembled monolayers (SAMs). J. Colloid Interface Sci. 185 (1997) 94-103
    • (1997) J. Colloid Interface Sci. , vol.185 , pp. 94-103
    • Silin, V.1    Weetall, H.2    Vanderah, D.J.3
  • 44
    • 0023825805 scopus 로고    scopus 로고
    • Protein adsorption on functionalized and ESCA-characterized polymer films studied by ellipsometry
    • Gölander C.-G., and Kiss E. Protein adsorption on functionalized and ESCA-characterized polymer films studied by ellipsometry. J. Colloid Interface Sci. 121 (1998) 240-253
    • (1998) J. Colloid Interface Sci. , vol.121 , pp. 240-253
    • Gölander, C.-G.1    Kiss, E.2


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