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Volumn 408, Issue 2, 2011, Pages 212-219

Direct detection of acetylcholinesterase inhibitor binding with an enzyme-based surface plasmon resonance sensor

Author keywords

Acetylcholinesterase inhibitors; Direct sensor; Surface plasmon resonance

Indexed keywords

BINDING ENERGY; CHEMICAL DETECTION; ENZYMES; NEURODEGENERATIVE DISEASES; PLASMONS; RESONANCE;

EID: 78149407717     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.09.009     Document Type: Article
Times cited : (49)

References (44)
  • 1
    • 78149406184 scopus 로고    scopus 로고
    • Goodman & Gilman's The Pharmacological Basis of Therapeutics, 11th ed. McGraw-Hill, New York, L.L. Brunton, J.S. Lazo, K.L. Parker (Eds.)
    • L.L. Brunton, J.S. Lazo, K.L. Parker (Eds.), Goodman & Gilman's The Pharmacological Basis of Therapeutics, 11th ed. McGraw-Hill
    • (2006)
  • 3
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
    • Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 1991, 253:872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 4
    • 77956895752 scopus 로고
    • Acetylcholinesterase
    • Academic Press, New York
    • Froede H.C., Wilson I.B. Acetylcholinesterase. The Enzymes, 3rd ed. 1971, vol. 5:87-114. Academic Press, New York.
    • (1971) The Enzymes, 3rd ed. , vol.5 , pp. 87-114
    • Froede, H.C.1    Wilson, I.B.2
  • 5
    • 0022899577 scopus 로고
    • Oral tetrahydroaminoacridine in long-term treatment of senile dementia, Alzheimer type
    • Summers W.K., Majovski L.V., Marsh G.M., Tachiki K., Kling A. Oral tetrahydroaminoacridine in long-term treatment of senile dementia, Alzheimer type. N. Engl. J. Med. 1986, 315:1241-1245.
    • (1986) N. Engl. J. Med. , vol.315 , pp. 1241-1245
    • Summers, W.K.1    Majovski, L.V.2    Marsh, G.M.3    Tachiki, K.4    Kling, A.5
  • 6
    • 0002994207 scopus 로고
    • Second and third generation cholinesterase inhibitors: From preclinical studies to clinical efficacy
    • Birkhauser Press, Boston, E. Giacobini, R. Becker (Eds.)
    • Giacobini E., Cuadra G. Second and third generation cholinesterase inhibitors: From preclinical studies to clinical efficacy. Alzheimer Disease: Therapeutic Strategies 1994, 155-171. Birkhauser Press, Boston. E. Giacobini, R. Becker (Eds.).
    • (1994) Alzheimer Disease: Therapeutic Strategies , pp. 155-171
    • Giacobini, E.1    Cuadra, G.2
  • 7
    • 0015885733 scopus 로고
    • Neuromuscular junction in myasthenia gravis: decreased acetylcholine receptors
    • Fambrough D.M., Drachman D.B., Satyamurti S. Neuromuscular junction in myasthenia gravis: decreased acetylcholine receptors. Science 1973, 182:293-295.
    • (1973) Science , vol.182 , pp. 293-295
    • Fambrough, D.M.1    Drachman, D.B.2    Satyamurti, S.3
  • 8
    • 0025755348 scopus 로고
    • Alzheimer disease: basic and clinical advances
    • Katzman R., Jackson J.E. Alzheimer disease: basic and clinical advances. J. Am. Geriatr. Soc. 1991, 39:516-525.
    • (1991) J. Am. Geriatr. Soc. , vol.39 , pp. 516-525
    • Katzman, R.1    Jackson, J.E.2
  • 10
    • 0028896261 scopus 로고
    • Chemiluminescence assays of organophosphorus and carbamate pesticides
    • Moris P., Alexandre I., Roger M., Remacle J. Chemiluminescence assays of organophosphorus and carbamate pesticides. Anal. Chim. 1995, 302:53-59.
    • (1995) Anal. Chim. , vol.302 , pp. 53-59
    • Moris, P.1    Alexandre, I.2    Roger, M.3    Remacle, J.4
  • 11
  • 12
    • 0028854253 scopus 로고
    • Characterization of inhibitors of acetylcholinesterase by an automated amperometric flow-injection system
    • Guenther A., Bilitewski U. Characterization of inhibitors of acetylcholinesterase by an automated amperometric flow-injection system. Anal. Chim. Acta 1995, 300:117-125.
    • (1995) Anal. Chim. Acta , vol.300 , pp. 117-125
    • Guenther, A.1    Bilitewski, U.2
  • 13
    • 0026740147 scopus 로고
    • An enzyme-reactor for electrochemical monitoring of choline and acetylcholine: applications in high-performance liquid chromatography, brain tissue, microdialysis, and cerebrospinal fluid
    • Flentge F., Venema K., Koch T., Korf J. An enzyme-reactor for electrochemical monitoring of choline and acetylcholine: applications in high-performance liquid chromatography, brain tissue, microdialysis, and cerebrospinal fluid. Anal. Biochem. 1992, 204:305-310.
    • (1992) Anal. Biochem. , vol.204 , pp. 305-310
    • Flentge, F.1    Venema, K.2    Koch, T.3    Korf, J.4
  • 14
    • 33750438054 scopus 로고    scopus 로고
    • Nonfaradaic impedance probing of potato glycoalkaloids interaction with butyrylcholinesterase immobilized onto gold electrode
    • Benilova I.V., Soldatkin A.P., Martelet C., Jaffrezic-Renault N. Nonfaradaic impedance probing of potato glycoalkaloids interaction with butyrylcholinesterase immobilized onto gold electrode. Electroanalysis 2006, 18:1950-1956.
    • (2006) Electroanalysis , vol.18 , pp. 1950-1956
    • Benilova, I.V.1    Soldatkin, A.P.2    Martelet, C.3    Jaffrezic-Renault, N.4
  • 15
    • 0032626631 scopus 로고    scopus 로고
    • Surface plasmon resonance sensors: review
    • Homola J., Yee S.S., Gauglitz G. Surface plasmon resonance sensors: review. Sens. Actuat. B 1999, 54:3-15.
    • (1999) Sens. Actuat. B , vol.54 , pp. 3-15
    • Homola, J.1    Yee, S.S.2    Gauglitz, G.3
  • 16
    • 0031534443 scopus 로고    scopus 로고
    • Detection of morphine in ppb range by using SPR (surface plasmon resonance) immunosensor
    • Miura N., Ogata K., Sakai G., Uda T., Yamazoe N. Detection of morphine in ppb range by using SPR (surface plasmon resonance) immunosensor. Chem. Lett. 1997, 713-714.
    • (1997) Chem. Lett. , pp. 713-714
    • Miura, N.1    Ogata, K.2    Sakai, G.3    Uda, T.4    Yamazoe, N.5
  • 17
    • 84958310303 scopus 로고
    • Detection of pesticide in drinking water using real-time biospecific interaction analysis (BIA)
    • Minunni M., Mascini M. Detection of pesticide in drinking water using real-time biospecific interaction analysis (BIA). Anal. Lett. 1993, 26:1441-1460.
    • (1993) Anal. Lett. , vol.26 , pp. 1441-1460
    • Minunni, M.1    Mascini, M.2
  • 18
    • 0344177897 scopus 로고    scopus 로고
    • Present and future of surface plasmon resonance biosensors
    • Homola J. Present and future of surface plasmon resonance biosensors. Anal. Bioanal. Chem. 2003, 377:528-539.
    • (2003) Anal. Bioanal. Chem. , vol.377 , pp. 528-539
    • Homola, J.1
  • 19
    • 34247635052 scopus 로고    scopus 로고
    • Surface plasmon resonance based fiber-optic sensor for the detection of pesticide
    • Jha R., Chand S., Gupta B.D. Surface plasmon resonance based fiber-optic sensor for the detection of pesticide. Sens. Actuat. B 2007, 123:661-666.
    • (2007) Sens. Actuat. B , vol.123 , pp. 661-666
    • Jha, R.1    Chand, S.2    Gupta, B.D.3
  • 20
    • 16244391144 scopus 로고    scopus 로고
    • Improved method for the preparation of carboxylic acid and amine terminated self-assembled monolayers of alkanethiolates
    • Wang H., Chen S., Li L., Jiang S. Improved method for the preparation of carboxylic acid and amine terminated self-assembled monolayers of alkanethiolates. Langmuir 2005, 21:2633-2636.
    • (2005) Langmuir , vol.21 , pp. 2633-2636
    • Wang, H.1    Chen, S.2    Li, L.3    Jiang, S.4
  • 21
    • 1942481178 scopus 로고
    • Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold
    • Bain C.D., Troughton E.B., Tao Y.T., Evall J., Whitesides G.M., Nuzzo R.G. Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold. J. Am. Chem. Soc. 1989, 111:321-335.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 321-335
    • Bain, C.D.1    Troughton, E.B.2    Tao, Y.T.3    Evall, J.4    Whitesides, G.M.5    Nuzzo, R.G.6
  • 23
    • 0033557842 scopus 로고    scopus 로고
    • A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study
    • Lahiri J., Isaacs L., Tien J., Whitesides G.M. A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study. Anal. Chem. 1999, 71:777-790.
    • (1999) Anal. Chem. , vol.71 , pp. 777-790
    • Lahiri, J.1    Isaacs, L.2    Tien, J.3    Whitesides, G.M.4
  • 26
    • 18044398972 scopus 로고    scopus 로고
    • Self-assembled monolayers of thiolates on metals as a form of nanotechnology
    • Love J.C., Estroff L.A., Kriebel J.K., Nuzzo R.G., Whitesides G.M. Self-assembled monolayers of thiolates on metals as a form of nanotechnology. Chem. Rev. 2005, 105:1103-1169.
    • (2005) Chem. Rev. , vol.105 , pp. 1103-1169
    • Love, J.C.1    Estroff, L.A.2    Kriebel, J.K.3    Nuzzo, R.G.4    Whitesides, G.M.5
  • 27
    • 0345979435 scopus 로고    scopus 로고
    • Formation and structure of self-assembled monolayers
    • Ulman A. Formation and structure of self-assembled monolayers. Chem. Rev. 1996, 96:1533-1554.
    • (1996) Chem. Rev. , vol.96 , pp. 1533-1554
    • Ulman, A.1
  • 28
    • 9144268627 scopus 로고    scopus 로고
    • Reactive self-assembled monolayers on flat and nanoparticle surfaces, and their application in soft and scanning probe lithographic nanofabrication technologies
    • Li X.-M., Huskens J., Reinhoudt D.N. Reactive self-assembled monolayers on flat and nanoparticle surfaces, and their application in soft and scanning probe lithographic nanofabrication technologies. J. Mater. Chem. 2004, 14:2954-2971.
    • (2004) J. Mater. Chem. , vol.14 , pp. 2954-2971
    • Li, X.-M.1    Huskens, J.2    Reinhoudt, D.N.3
  • 30
    • 0031269226 scopus 로고    scopus 로고
    • Immobilization of protein molecules onto homogeneous and mixed carboxylate-terminated self-assembled monolayers
    • Patel N., Davies M.C., Hartshorne M., Heaton R.J., Roberts C.J., Tendler S.J.B., Williams P.M. Immobilization of protein molecules onto homogeneous and mixed carboxylate-terminated self-assembled monolayers. Langmuir 1997, 13:6485-6490.
    • (1997) Langmuir , vol.13 , pp. 6485-6490
    • Patel, N.1    Davies, M.C.2    Hartshorne, M.3    Heaton, R.J.4    Roberts, C.J.5    Tendler, S.J.B.6    Williams, P.M.7
  • 31
    • 0033204169 scopus 로고    scopus 로고
    • Biospecific binding of carbonic anhydrase to mixed SAMs presenting benzenesulfonamide ligands: a model system for studying lateral steric effects
    • Lahiri J., Isaacs L., Grzybowski B., Carbeck J.D., Whitesides G.M. Biospecific binding of carbonic anhydrase to mixed SAMs presenting benzenesulfonamide ligands: a model system for studying lateral steric effects. Langmuir 1999, 15:7186-7198.
    • (1999) Langmuir , vol.15 , pp. 7186-7198
    • Lahiri, J.1    Isaacs, L.2    Grzybowski, B.3    Carbeck, J.D.4    Whitesides, G.M.5
  • 32
    • 0001245792 scopus 로고
    • A study by contact angle of the acid-base behavior of monolayers containing ω-mercaptocarboxylic acids adsorbed on gold: an example of reactive spreading
    • Bain C.D., Whitesides G.M. A study by contact angle of the acid-base behavior of monolayers containing ω-mercaptocarboxylic acids adsorbed on gold: an example of reactive spreading. Langmuir 1989, 5:1370-1378.
    • (1989) Langmuir , vol.5 , pp. 1370-1378
    • Bain, C.D.1    Whitesides, G.M.2
  • 33
    • 0028521764 scopus 로고
    • Contact-angle titrations of mixed ω-mercaptoalkanoic acid/alkanethiol monolayers on gold: reactive vs. nonreactive spreading, and chain length effects on surface pKa values
    • Creager S.E., Clarke J. Contact-angle titrations of mixed ω-mercaptoalkanoic acid/alkanethiol monolayers on gold: reactive vs. nonreactive spreading, and chain length effects on surface pKa values. Langmuir 1994, 10:3675-3683.
    • (1994) Langmuir , vol.10 , pp. 3675-3683
    • Creager, S.E.1    Clarke, J.2
  • 35
    • 0033573104 scopus 로고    scopus 로고
    • Dithiobissuccinimidyl propionate as an anchor for assembling peroxidases at electrode surfaces and its application in a H2O2 biosensor
    • Darder M., Takada K., Pariente F., Lorenzo E., Abruna H.D. Dithiobissuccinimidyl propionate as an anchor for assembling peroxidases at electrode surfaces and its application in a H2O2 biosensor. Anal. Chem. 1999, 71:5530-5537.
    • (1999) Anal. Chem. , vol.71 , pp. 5530-5537
    • Darder, M.1    Takada, K.2    Pariente, F.3    Lorenzo, E.4    Abruna, H.D.5
  • 36
    • 0034663437 scopus 로고    scopus 로고
    • Biosensors based on membrane-bound enzymes immobilized in a 5-(octyldithio)-2-nitrobenzoic acid layer on gold electrodes
    • Darder M., Casero E., Pariente F., Lorenzo E. Biosensors based on membrane-bound enzymes immobilized in a 5-(octyldithio)-2-nitrobenzoic acid layer on gold electrodes. Anal. Chem. 2000, 72:3784-3792.
    • (2000) Anal. Chem. , vol.72 , pp. 3784-3792
    • Darder, M.1    Casero, E.2    Pariente, F.3    Lorenzo, E.4
  • 37
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins
    • Stenberg E., Persson B., Roos H., Urbaniczky C. Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J. Colloid Interface Sci. 1991, 143:513-526.
    • (1991) J. Colloid Interface Sci. , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4
  • 38
    • 0032190343 scopus 로고    scopus 로고
    • The " aromatic patch" of three proximal residues in the human acetylcholinesterase active center allows for versatile interaction modes with inhibitors
    • Ariel N., Ordentlich A., Barak D., Bino T., Velan B., Shafferman A. The " aromatic patch" of three proximal residues in the human acetylcholinesterase active center allows for versatile interaction modes with inhibitors. Biochem. J. 1998, 335:95-102.
    • (1998) Biochem. J. , vol.335 , pp. 95-102
    • Ariel, N.1    Ordentlich, A.2    Barak, D.3    Bino, T.4    Velan, B.5    Shafferman, A.6
  • 39
    • 0032029432 scopus 로고    scopus 로고
    • Protein adsorption and ellipsometry in biomaterial research
    • Elwing H. Protein adsorption and ellipsometry in biomaterial research. Biomaterials 1998, 19:397-406.
    • (1998) Biomaterials , vol.19 , pp. 397-406
    • Elwing, H.1
  • 40
    • 0032523411 scopus 로고    scopus 로고
    • Detection of conformational changes in an immobilized protein using surface plasmon resonance
    • Sota H., Hasegawa Y., Iwakura M. Detection of conformational changes in an immobilized protein using surface plasmon resonance. Anal. Chem. 1998, 70:2019-2024.
    • (1998) Anal. Chem. , vol.70 , pp. 2019-2024
    • Sota, H.1    Hasegawa, Y.2    Iwakura, M.3
  • 41
    • 0033981950 scopus 로고    scopus 로고
    • High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins
    • Boussaad S., Pean J., Tao N.J. High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins. Anal. Chem. 2000, 72:222-226.
    • (2000) Anal. Chem. , vol.72 , pp. 222-226
    • Boussaad, S.1    Pean, J.2    Tao, N.J.3
  • 42
    • 0033747206 scopus 로고    scopus 로고
    • Plasmon resonance studies of agonist/antagonist binding to the human δ-opioid receptor: new structural insights into receptor-ligand interactions
    • Salamon Z., Cowell S., Varga E., Yamamura H.I., Hruby V.J., Tollin G. Plasmon resonance studies of agonist/antagonist binding to the human δ-opioid receptor: new structural insights into receptor-ligand interactions. Biophys. J. 2000, 79:2463-2474.
    • (2000) Biophys. J. , vol.79 , pp. 2463-2474
    • Salamon, Z.1    Cowell, S.2    Varga, E.3    Yamamura, H.I.4    Hruby, V.J.5    Tollin, G.6
  • 43
    • 0035584032 scopus 로고    scopus 로고
    • Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance
    • Gestwicki J.E., Hsieh H.V., Pitner J.B. Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance. Anal. Chem. 2001, 73:5732-5737.
    • (2001) Anal. Chem. , vol.73 , pp. 5732-5737
    • Gestwicki, J.E.1    Hsieh, H.V.2    Pitner, J.B.3
  • 44
    • 2542474493 scopus 로고    scopus 로고
    • Analysis of small-molecule interactions using Biacore S51 technology
    • Myszka D.G. Analysis of small-molecule interactions using Biacore S51 technology. Anal. Biochem. 2004, 329:316-323.
    • (2004) Anal. Biochem. , vol.329 , pp. 316-323
    • Myszka, D.G.1


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