메뉴 건너뛰기




Volumn 26, Issue 1, 2010, Pages 93-100

Amyloid fibrils as a nanoscaffold for enzyme immobilization

Author keywords

Amyloid; Cross linking; Glucose oxidase; Glutaraldehyde; Pvoh

Indexed keywords

AMYLOID FIBRIL; ANTI-BACTERIAL ACTIVITY; ANTIBACTERIAL EFFECTS; DENATURING CONDITIONS; E. COLI; FUNCTIONALIZATIONS; FUNCTIONALIZED; GLUTARALDEHYDES; NANOMETER SIZE; NANOSCAFFOLDS; PROOF OF CONCEPT; SUCROSE GRADIENTS; TEM;

EID: 76849113758     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.309     Document Type: Article
Times cited : (72)

References (41)
  • 3
    • 2942744730 scopus 로고    scopus 로고
    • Amyloid fibrils in bionanotechnology
    • Waterhouse SH, Gerrard JA. Amyloid fibrils in bionanotechnology. Aust J Chem. 2004;57:519-523.
    • (2004) Aust J Chem , vol.57 , pp. 519-523
    • Waterhouse, S.H.1    Gerrard, J.A.2
  • 4
    • 34249739081 scopus 로고    scopus 로고
    • Amyloid fibrils: From disease to design. New biomaterial applications for self-assembling cross-b fibrils
    • Gras SL. Amyloid fibrils: from disease to design. New biomaterial applications for self-assembling cross-b fibrils. Aust J Chem. 2007;60:333-342.
    • (2007) Aust J Chem , vol.60 , pp. 333-342
    • Gras, S.L.1
  • 5
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: Not only pathological agents but also ordered nanomaterials
    • Cherny I, Gazit E. Amyloids: not only pathological agents but also ordered nanomaterials. Angew Chem Int Edit. 2008;47: 4062-4069.
    • (2008) Angew Chem Int Edit , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 6
    • 0347285533 scopus 로고    scopus 로고
    • Kinetic behaviour and stability of glucose oxidase entrapped in liposomes
    • Rodriguez-Nogales JM. Kinetic behaviour and stability of glucose oxidase entrapped in liposomes. J Chem Technol Biotechnol. 2004;79:72-78.
    • (2004) J Chem Technol Biotechnol , vol.79 , pp. 72-78
    • Rodriguez-Nogales, J.M.1
  • 8
    • 0042591234 scopus 로고    scopus 로고
    • Thermal inactivation of glucose oxidase: Mechanism and stabilisation using additives
    • Gouda MD, Singh SA, Rao AGA, Thakur MS, Karanth NG. Thermal inactivation of glucose oxidase: mechanism and stabilisation using additives. J Biol Chem. 2003;278:24324-24333.
    • (2003) J Biol Chem , vol.278 , pp. 24324-24333
    • Gouda, M.D.1    Singh, S.A.2    Rao, A.G.A.3    Thakur, M.S.4    Karanth, N.G.5
  • 9
    • 43549095197 scopus 로고    scopus 로고
    • Glucose oxidase: Natural occurrence, function, properties and industrial applications
    • Wong CM, Wong KH, Chen XD. Glucose oxidase: natural occurrence, function, properties and industrial applications. Appl Microbiol Biotechnol. 2008;78:927-938.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 927-938
    • Wong, C.M.1    Wong, K.H.2    Chen, X.D.3
  • 11
    • 0037411503 scopus 로고    scopus 로고
    • Immobilisation of glucose oxidase within metallic nanotubes arrays for application to enzyme biosensors
    • Delvaux M, Demoustier-Champagne S. Immobilisation of glucose oxidase within metallic nanotubes arrays for application to enzyme biosensors. Biosens Bioelectron. 2003;8:943-951.
    • (2003) Biosens Bioelectron , vol.8 , pp. 943-951
    • Delvaux, M.1    Demoustier-Champagne, S.2
  • 12
    • 37349119751 scopus 로고    scopus 로고
    • A novel glucose biosensor based on immobilization of glucose oxidase into multiwall carbon nanotubes-polyelectrolyte-loaded electrospun nanofibrous membrane
    • Manesh KM, Kim HT, Santhosh P. Gopalan AI, Lee K-P. A novel glucose biosensor based on immobilization of glucose oxidase into multiwall carbon nanotubes-polyelectrolyte-loaded electrospun nanofibrous membrane. Biosens Bioelectron. 2008; 23:771-779.
    • (2008) Biosens Bioelectron , vol.23 , pp. 771-779
    • Manesh, K.M.1    Kim, H.T.2    Santhosh, P.3    Gopalan, A.I.4    Lee, K.-P.5
  • 13
    • 38749142558 scopus 로고    scopus 로고
    • Comparative study of poly(vinyl alcohol)-based support materials for the immobilization of glucose oxidase
    • Wong F-L, Abdul-Aziz A. Comparative study of poly(vinyl alcohol)-based support materials for the immobilization of glucose oxidase. J Chem Technol Biotechnol. 2008;83:41-46.
    • (2008) J Chem Technol Biotechnol , vol.83 , pp. 41-46
    • Wong, F.-L.1    Abdul-Aziz, A.2
  • 14
    • 38549099702 scopus 로고    scopus 로고
    • Micropatterning of proteins on the surface of three-dimensional poly(ethylene glycol) hydrogel microstructures
    • Kim D-N, Lee W, Koh W-G. Micropatterning of proteins on the surface of three-dimensional poly(ethylene glycol) hydrogel microstructures. Anal Chim Acta. 2008;609:59-65.
    • (2008) Anal Chim Acta , vol.609 , pp. 59-65
    • Kim, D.-N.1    Lee, W.2    Koh, W.-G.3
  • 15
    • 27644525074 scopus 로고    scopus 로고
    • Antimicrobial activity of glucose oxidase-immobilized plasma-activated polypropylene films
    • Vartiainen J, Rátto M, Paulussen S. Antimicrobial activity of glucose oxidase-immobilized plasma-activated polypropylene films. Packag Technol Sci. 2005;18:243-251.
    • (2005) Packag Technol Sci , vol.18 , pp. 243-251
    • Vartiainen, J.1    Rátto, M.2    Paulussen, S.3
  • 16
    • 33751000228 scopus 로고    scopus 로고
    • Immobilization of GOD on electro-chemically synthesized Ppy-PVS composite film by cross-linking via glutaraldehyde for determination of glucose
    • Gade VK, Shirale DJ, Gaikwad PD, Savale PA, Kakde KP, Kharat HJ, Shirsat MD. Immobilization of GOD on electro-chemically synthesized Ppy-PVS composite film by cross-linking via glutaraldehyde for determination of glucose. React Funct Polym. 2006;66:1420-1426.
    • (2006) React Funct Polym , vol.66 , pp. 1420-1426
    • Gade, V.K.1    Shirale, D.J.2    Gaikwad, P.D.3    Savale, P.A.4    Kakde, K.P.5    Kharat, H.J.6    Shirsat, M.D.7
  • 17
    • 0035158241 scopus 로고    scopus 로고
    • Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy
    • Nielsen L, Frokjaer S, Carpenter JF, Brange J. Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy. J Pharm Sci. 2001;90: 29-37.
    • (2001) J Pharm Sci , vol.90 , pp. 29-37
    • Nielsen, L.1    Frokjaer, S.2    Carpenter, J.F.3    Brange, J.4
  • 18
    • 0027502784 scopus 로고
    • Thioflavine T. interaction with synthetic Alzheimer's disease b-amyloid peptides: Detection of amyloid aggregation in solution
    • Levine H III, Thioflavine T. interaction with synthetic Alzheimer's disease b-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 1993;2:404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • Levine, H.I.I.I.1
  • 19
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of b-sheet amyloid fibril structures with thioflavin T
    • Levine H III. Quantification of b-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 1999;309:274-284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • Levine III, H.1
  • 20
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • Zhou M, Diwu Z, Panchuk-Voloshina N, Haugland RP. A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal Biochem. 1997;253:162-168.
    • (1997) Anal Biochem , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 21
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • Schrodel A, De Marco A. Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem. 2005;6:10.
    • (2005) Bmc Biochem , vol.6 , pp. 10
    • Schrodel, A.1    de Marco, A.2
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem. 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0015517217 scopus 로고
    • Cross-b protein structures. I. Insulin fibrils
    • Burke MJ, Rougvie MA. Cross-b protein structures. I. Insulin fibrils. Biochemistry 1972;11:2435-2439.
    • (1972) Biochemistry , vol.11 , pp. 2435-2439
    • Burke, M.J.1    Rougvie, M.A.2
  • 25
    • 76849099981 scopus 로고    scopus 로고
    • School of Biological Sciences, PhD Thesis, University of Canterbury, Christchurch
    • Rao SP. Amyloid fibrils in bionanomaterials. School of Biological Sciences, PhD Thesis, University of Canterbury, Christchurch, 2008.
    • (2008) Amyloid Fibrils In Bionanomaterials
    • Rao, S.P.1
  • 27
    • 2442715309 scopus 로고    scopus 로고
    • Mechanism of insulin fibrillation: The structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate
    • Hua Q-X, Weiss MA. Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate. J Biol Chem. 2004;279:21449-21460.
    • (2004) J Biol Chem , vol.279 , pp. 21449-21460
    • Hua, Q.-X.1    Weiss, M.A.2
  • 28
    • 30044446633 scopus 로고    scopus 로고
    • Early in the fibrillation of monomeric insulin
    • Ahmad A, Uversky VN, Hong D, Fink AL. Early in the fibrillation of monomeric insulin. J Biol Chem. 2005;280:2669-42675.
    • (2005) J Biol Chem , vol.280 , pp. 2669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 30
    • 1242299760 scopus 로고    scopus 로고
    • Electrochemical bio-sensing platforms using platinum nanoparticles and carbon nanotubes
    • Hrapovic S, Liu Y, Male KB, Luong JHT. Electrochemical bio-sensing platforms using platinum nanoparticles and carbon nanotubes. Anal Chem. 2004;76:1083-1088.
    • (2004) Anal Chem , vol.76 , pp. 1083-1088
    • Hrapovic, S.1    Liu, Y.2    Male, K.B.3    Luong, J.H.T.4
  • 31
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson MR. Techniques to study amyloid fibril formation in vitro. Methods. 2004;34:151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 32
    • 13444310821 scopus 로고    scopus 로고
    • Glucose oxidase from Aspergillus niger: The mechanism of action with molecular oxygen, quinones, and one-electron acceptors
    • Leskovac V, Trivic S, Wohlfahrt G, Kandrac J, Perićin D. Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors. Int J Biochem Cell Biol. 2005;37:731-750.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 731-750
    • Leskovac, V.1    Trivic, S.2    Wohlfahrt, G.3    Kandrac, J.4    Perićin, D.5
  • 33
    • 0036740603 scopus 로고    scopus 로고
    • Stabilization of activity of oxidoreductases by their immobilization onto special functionalized glass and novel aminocellulose film using different coupling reagents
    • Tiller JC, Rieseler R, Berlin P, Klemm D. Stabilization of activity of oxidoreductases by their immobilization onto special functionalized glass and novel aminocellulose film using different coupling reagents. Biomacromolecules 2002;3:1021-1029.
    • (2002) Biomacromolecules , vol.3 , pp. 1021-1029
    • Tiller, J.C.1    Rieseler, R.2    Berlin, P.3    Klemm, D.4
  • 34
    • 0037235778 scopus 로고    scopus 로고
    • Competitive inhibition by hydrogen peroxide produced in glucose oxidation catalyzed by glucose oxidase
    • Bao J, Furumoto K, Yoshimoto M, Fukunaga K, Nakao K. Competitive inhibition by hydrogen peroxide produced in glucose oxidation catalyzed by glucose oxidase. Biochem Eng J. 2003;13:69-72.
    • (2003) Biochem Eng J , vol.13 , pp. 69-72
    • Bao, J.1    Furumoto, K.2    Yoshimoto, M.3    Fukunaga, K.4    Nakao, K.5
  • 35
    • 0017079753 scopus 로고    scopus 로고
    • The construction and analysis of sucrose gradients for use with zonal rotors
    • Hirst W, Cox RA. The construction and analysis of sucrose gradients for use with zonal rotors. Biochem J. 76:259-265.
    • Biochem J , vol.76 , pp. 259-265
    • Hirst, W.1    Cox, R.A.2
  • 36
    • 48549088501 scopus 로고    scopus 로고
    • An easy method using glutaraldehyde-introduced fluorescence for the microscopic analysis of plant biotrophic interactions
    • Fester T, Berg RH, Taylor CG. An easy method using glutaraldehyde-introduced fluorescence for the microscopic analysis of plant biotrophic interactions. J Microsc. 2008;231:342-348.
    • (2008) J Microsc , vol.231 , pp. 342-348
    • Fester, T.1    Berg, R.H.2    Taylor, C.G.3
  • 37
    • 0027272553 scopus 로고
    • The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme
    • Hecht HJ, Schomburg D, Kalisz H, Schmid RD. The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme. Biosens Bioelectron. 1993;8:197-203.
    • (1993) Biosens Bioelectron , vol.8 , pp. 197-203
    • Hecht, H.J.1    Schomburg, D.2    Kalisz, H.3    Schmid, R.D.4
  • 38
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, Detitta GT, Dekker N, Nordlund P. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem. 2006;357:289-298.
    • (2006) Anal Biochem , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 39
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2007;2:2212-2221.
    • (2007) Nat Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 40
    • 0035964991 scopus 로고    scopus 로고
    • Inhibitory activity of honey against foodborne pathogens as influenced by the presence of hydrogen peroxide and level of antioxidant power
    • Taormina PJ, Niemira BA, Beuchat LR. Inhibitory activity of honey against foodborne pathogens as influenced by the presence of hydrogen peroxide and level of antioxidant power. Int J Food Microbiol. 2001;69:217-225.
    • (2001) Int J Food Microbiol , vol.69 , pp. 217-225
    • Taormina, P.J.1    Niemira, B.A.2    Beuchat, L.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.