메뉴 건너뛰기




Volumn 17, Issue 6, 2006, Pages 1373-1375

Bionanoconjugation via click chemistry: The creation of functional hybrids of lipases and gold nanoparticles

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; FIBER OPTIC SENSORS; GOLD NANOPARTICLES; LIPASES;

EID: 33845217955     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc0601018     Document Type: Article
Times cited : (248)

References (38)
  • 1
    • 1842484779 scopus 로고    scopus 로고
    • Designing materials for biology and medicine
    • Langer, R., and Tirrell, D. A. (2004) Designing materials for biology and medicine. Nature (London) 428, 487-492.
    • (2004) Nature (London) , vol.428 , pp. 487-492
    • Langer, R.1    Tirrell, D.A.2
  • 2
    • 14044274098 scopus 로고    scopus 로고
    • On the development of colloidal nanoparticles towards multifunctional structures and their possible use for biological applications
    • Pellegrino, T., Kudera, S., Liedl, T., Munoz, H. A., Manna, L., and Parak, W. J. (2005) On the development of colloidal nanoparticles towards multifunctional structures and their possible use for biological applications. Small 1, 48-63.
    • (2005) Small , vol.1 , pp. 48-63
    • Pellegrino, T.1    Kudera, S.2    Liedl, T.3    Munoz, H.A.4    Manna, L.5    Parak, W.J.6
  • 3
    • 17944366258 scopus 로고    scopus 로고
    • Nanostructures in biodiagnostics
    • Rosi, N. L., and Mirkin, C. A. (2005) Nanostructures in biodiagnostics. Chem. Rev. 105, 1547-1562.
    • (2005) Chem. Rev. , vol.105 , pp. 1547-1562
    • Rosi, N.L.1    Mirkin, C.A.2
  • 5
    • 13844297094 scopus 로고    scopus 로고
    • The impact of nanobiotechnology on the development of new drug delivery systems
    • Kayser, O., Lemke, A., and Hernandez-Trejo, N. (2005) The impact of nanobiotechnology on the development of new drug delivery systems. Curr. Pharm. Biotechnol. 6, 3-5.
    • (2005) Curr. Pharm. Biotechnol. , vol.6 , pp. 3-5
    • Kayser, O.1    Lemke, A.2    Hernandez-Trejo, N.3
  • 6
    • 0035131970 scopus 로고    scopus 로고
    • Nanoengineering of particle surfaces
    • Caruso, F. (2001) Nanoengineering of particle surfaces. Adv. Mater. 13, 11-22.
    • (2001) Adv. Mater. , vol.13 , pp. 11-22
    • Caruso, F.1
  • 7
    • 0346725932 scopus 로고    scopus 로고
    • The use of nanocrystals in biological detection
    • Alivisatos, A. P. (2004) The use of nanocrystals in biological detection. Nat. Biotechnol. 22, 47-52.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 47-52
    • Alivisatos, A.P.1
  • 10
    • 17644397303 scopus 로고    scopus 로고
    • Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins
    • Abad, J. M., Mertens, S. F. L., Pita, M., Fernandez, V. M., and Schiffrin, D. J. (2005) Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins. J. Am. Chem. Soc. 127, 5689-5694.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5689-5694
    • Abad, J.M.1    Mertens, S.F.L.2    Pita, M.3    Fernandez, V.M.4    Schiffrin, D.J.5
  • 11
    • 3042774282 scopus 로고    scopus 로고
    • Enzyme-catalyzed bio-pumping of electrons into Au-nanoparticles: A surface plasmon resonance and electrochemical study
    • Liobashevski, O., Chegel, V. I., Patolsky, F., Katz, E., and Willner, I. (2004) Enzyme-catalyzed bio-pumping of electrons into Au-nanoparticles: a surface plasmon resonance and electrochemical study. J. Am. Chem. Soc. 126, 7133-7143.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7133-7143
    • Liobashevski, O.1    Chegel, V.I.2    Patolsky, F.3    Katz, E.4    Willner, I.5
  • 12
    • 29844434629 scopus 로고    scopus 로고
    • Gold nanoparticle-cytochrome c complexes: The effect of nanoparticle ligand charge on protein structure
    • Aubin-Tam, M. E., and Hamad-Schifferli, K. (2005) Gold nanoparticle-cytochrome c complexes: the effect of nanoparticle ligand charge on protein structure. Langmuir 21, 12080-12084.
    • (2005) Langmuir , vol.21 , pp. 12080-12084
    • Aubin-Tam, M.E.1    Hamad-Schifferli, K.2
  • 13
    • 16244402954 scopus 로고    scopus 로고
    • Labelling ribonuclease S with a 3 nm Au nanoparticle by two-step assembly
    • Aubin, M. E., Morales, D. G., and Hamad-Schifferli, K. (2005) Labelling ribonuclease S with a 3 nm Au nanoparticle by two-step assembly. Nano Lett. 5, 519-522.
    • (2005) Nano Lett. , vol.5 , pp. 519-522
    • Aubin, M.E.1    Morales, D.G.2    Hamad-Schifferli, K.3
  • 14
    • 15744365262 scopus 로고    scopus 로고
    • Nanoparticle-based optical biosensors for the direct detection of organophosphate chemical warfare agents and pesticides
    • Simonian, A. L., Good, T. A., Wang, S.-.S., and Wild, J. R. (2005) Nanoparticle-based optical biosensors for the direct detection of organophosphate chemical warfare agents and pesticides. Anal. Chim. Acta 534, 69-77.
    • (2005) Anal. Chim. Acta , vol.534 , pp. 69-77
    • Simonian, A.L.1    Good, T.A.2    Wang, S.-S.3    Wild, J.R.4
  • 15
    • 23944440676 scopus 로고    scopus 로고
    • Immobilization of hexa-arginine tagged esterase onto carboxylated gold nanoparticles
    • Ha, T. H., Jeong, J. Y., and Chung, B. H. (2005) Immobilization of hexa-arginine tagged esterase onto carboxylated gold nanoparticles. Chem. Commun. 3959-3961.
    • (2005) Chem. Commun. , pp. 3959-3961
    • Ha, T.H.1    Jeong, J.Y.2    Chung, B.H.3
  • 16
    • 29444452750 scopus 로고    scopus 로고
    • Interaction of azide ion with hemin and cytochrome c immobilized on Au and Ag nanoparticles
    • Tom, R. T., and Pradeep, T. (2005) Interaction of azide ion with hemin and cytochrome c immobilized on Au and Ag nanoparticles. Langmuir 21, 11896-11902.
    • (2005) Langmuir , vol.21 , pp. 11896-11902
    • Tom, R.T.1    Pradeep, T.2
  • 17
    • 0026773640 scopus 로고
    • Comparison of colloidal gold electrode fabrication methods: The preparation of a horseradish peroxidase enzyme electrode
    • Stonehuerner, J. G., Zhao, J., O'Daly, J. P., Crumbliss, A. L., and Henkens, R. W. (1992) Comparison of colloidal gold electrode fabrication methods: the preparation of a horseradish peroxidase enzyme electrode. Biosens. Bioelectron. 7, 421-428.
    • (1992) Biosens. Bioelectron. , vol.7 , pp. 421-428
    • Stonehuerner, J.G.1    Zhao, J.2    O'Daly, J.P.3    Crumbliss, A.L.4    Henkens, R.W.5
  • 18
    • 4243998148 scopus 로고    scopus 로고
    • Protein: Colloid conjugates for surface-enhanced raman scattering: stability and control of protein orientation
    • Keating, C. D., Kovaleski, K. M., and Natan, M. J. (1998) Protein: colloid conjugates for surface-enhanced raman scattering: stability and control of protein orientation. J. Phys. Chem. B 102, 9404-9413.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 9404-9413
    • Keating, C.D.1    Kovaleski, K.M.2    Natan, M.J.3
  • 20
    • 0037117496 scopus 로고    scopus 로고
    • Inhibition of chymotrypsin through surface binding using nanoparticle-based receptors
    • Fisher, N. O., McIntosh, C. M., Simard, J. M., and Rotello, V. M. (2005) Inhibition of chymotrypsin through surface binding using nanoparticle-based receptors. Proc. Nat. Acad. Sci. U.S.A. 99, 5018-5023.
    • (2005) Proc. Nat. Acad. Sci. U.S.A. , vol.99 , pp. 5018-5023
    • Fisher, N.O.1    McIntosh, C.M.2    Simard, J.M.3    Rotello, V.M.4
  • 21
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • Rostovstev, V. V., Green, L. G., Fokin, V. F., and Sharpless, K. B. (2002) A stepwise Huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem., Int. Ed. 41, 2596-2599.
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 2596-2599
    • Rostovstev, V.V.1    Green, L.G.2    Fokin, V.F.3    Sharpless, K.B.4
  • 23
  • 24
    • 33744946037 scopus 로고    scopus 로고
    • Triazole cycloaddition as a general route for functionalization of Au nanoparticles
    • Fleming, D. A., Thode, C. J., Williams, M. E. (2006) Triazole cycloaddition as a general route for functionalization of Au nanoparticles. Chem. Mater. 18, 2327-2334.
    • (2006) Chem. Mater. , vol.18 , pp. 2327-2334
    • Fleming, D.A.1    Thode, C.J.2    Williams, M.E.3
  • 25
    • 19744370243 scopus 로고    scopus 로고
    • PEG- and peptide-grafted aliphatic polyesters by click chemistry
    • Parrish, B., Breitenkamp, R. B., and Emrick, T. (2005) PEG- and peptide-grafted aliphatic polyesters by click chemistry. J. Am. Chem. Soc. 127, 7404-7410.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7404-7410
    • Parrish, B.1    Breitenkamp, R.B.2    Emrick, T.3
  • 26
    • 28844480011 scopus 로고    scopus 로고
    • Shell click-crosslinked (SCC) nanoparticles: A new methodology for synthesis and orthogonal functionalization
    • Joralemon, M. J., O'Reilly, R. K., Hawker, C. J., and Wooley, K. L. (2005) Shell click-crosslinked (SCC) nanoparticles: a new methodology for synthesis and orthogonal functionalization. J. Am. Chem. Soc. 127, 16892-16899.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16892-16899
    • Joralemon, M.J.1    O'Reilly, R.K.2    Hawker, C.J.3    Wooley, K.L.4
  • 27
    • 33746096072 scopus 로고
    • A study of the nucleation and growth processes in the synthesis of colloidal gold
    • Turkevich, J., Stevenson, P. C., and Hillier, J. (1951) A study of the nucleation and growth processes in the synthesis of colloidal gold. Discuss. Faraday Soc. 11, 55-57.
    • (1951) Discuss. Faraday Soc. , vol.11 , pp. 55-57
    • Turkevich, J.1    Stevenson, P.C.2    Hillier, J.3
  • 28
    • 0003051583 scopus 로고
    • Controlled nucleation for regulation of particle-size in monodisperse gold suspensions
    • Frens, G. (1973) Controlled nucleation for regulation of particle-size in monodisperse gold suspensions. Nat. Phys. Sci. 241, 20-22.
    • (1973) Nat. Phys. Sci. , vol.241 , pp. 20-22
    • Frens, G.1
  • 29
    • 0037076648 scopus 로고    scopus 로고
    • Synthesis of hexanedithiolate/decanethiolate mixed monolayer protected gold clusters and scanning tunneling microscope induced patterning on the clusters/Au(111) surface
    • Yang, W., Chen, M., Knoll, W., and Deng, H. (2002) Synthesis of hexanedithiolate/decanethiolate mixed monolayer protected gold clusters and scanning tunneling microscope induced patterning on the clusters/Au(111) surface. Langmuir 18, 4124-4130.
    • (2002) Langmuir , vol.18 , pp. 4124-4130
    • Yang, W.1    Chen, M.2    Knoll, W.3    Deng, H.4
  • 30
    • 12044254336 scopus 로고
    • Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide) - A model system using self-assembled monolayers
    • Prime, K. L., and Whitesides, G. M. (1993) 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) J. Am. Chem. Soc. , vol.115 , pp. 10714-10721
    • Prime, K.L.1    Whitesides, G.M.2
  • 31
    • 4644308595 scopus 로고    scopus 로고
    • Nanoparticles comprising a mixed monolayer for specific bindings with biomolecules
    • Zheng, M., and Huang, X. (2004) Nanoparticles comprising a mixed monolayer for specific bindings with biomolecules. J. Am. Chem. Soc. 126, 12047-12054.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12047-12054
    • Zheng, M.1    Huang, X.2
  • 32
    • 0034731605 scopus 로고    scopus 로고
    • Lipase protein engineering
    • Svendsen, A. (2000) Lipase protein engineering. Biochim. Biophys. Acta 1543, 223-238.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 223-238
    • Svendsen, A.1
  • 35
    • 0035829832 scopus 로고    scopus 로고
    • Location of crosslinks in chemically stabilized horseradish peroxidase: Implications for design of crosslinks
    • O'Brien, A. M., O'Fágáin, C., Nielsen, P. F., and Welinder, K. G. (2001) Location of crosslinks in chemically stabilized horseradish peroxidase: implications for design of crosslinks. Biotechnol. Bioeng. 76, 277-284.
    • (2001) Biotechnol. Bioeng. , vol.76 , pp. 277-284
    • O'Brien, A.M.1    O'Fágáin, C.2    Nielsen, P.F.3    Welinder, K.G.4
  • 36
    • 0025200076 scopus 로고
    • Use of maleimide-thiol coupling chemistry for efficient synthesis of oligonucleotide-enzyme conjugate hybridization probes
    • Ghosh, S. S., Kao, P. M., McCue, A. W., and Chappelle, H. L. (1990) Use of maleimide-thiol coupling chemistry for efficient synthesis of oligonucleotide-enzyme conjugate hybridization probes. Bioconjugate Chem. 1, 71-76.
    • (1990) Bioconjugate Chem. , vol.1 , pp. 71-76
    • Ghosh, S.S.1    Kao, P.M.2    McCue, A.W.3    Chappelle, H.L.4
  • 37
    • 1642535341 scopus 로고    scopus 로고
    • Control of protein structure and function through surface recognition by tailored nanoparticle scaffolds
    • Hong, R., Emrick, N. O., Verna, A., Goodman, C. M., Emrick, T., and Rotello, V. M. (2004) Control of protein structure and function through surface recognition by tailored nanoparticle scaffolds. J. Am. Chem. Soc. 126, 739-743.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 739-743
    • Hong, R.1    Emrick, N.O.2    Verna, A.3    Goodman, C.M.4    Emrick, T.5    Rotello, V.M.6
  • 38
    • 0014660868 scopus 로고
    • Fluorometric substrate for sulfatase and lipase
    • Guilbault, G. G., and Hieserman, J. (1969) Fluorometric substrate for sulfatase and lipase. Anal. Chem. 41, 2006-2009.
    • (1969) Anal. Chem. , vol.41 , pp. 2006-2009
    • Guilbault, G.G.1    Hieserman, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.