Acetylcholinesterase capillary enzyme reactor for screening and characterization of selective inhibitors

Journal of Pharmaceutical and Biomedical Analysis

Volumn 73, Issue , 2013, Pages 44-52

  da Silva, Joyce Izidoro ^a   de Moraes, Marcela Cristina ^b   Vieira, Lucas Campos Curcino ^b   Corrêa, Arlene Gonçalves ^b   Cass, Quezia Bezerra ^b   Cardoso, Carmen Lucia ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b FEDERAL UNIVERSITY OF SÃO CARLOS   (Brazil)

Author keywords

Acetylcholinesterase; Coumarins derivatives; Immobilization; Screening; Silica capillary

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE INHIBITOR; COUMARIN DERIVATIVE; ETHYL 2 OXO 7 (2 PIPERIDIN 1 YLMETHYL) 2H CHROMENE 3 CARBOXYLATE; ETHYL 7 HYDROXY 2 OXO 8 (PIPERIDIN 1 YLMETHYL) 2H CHROMENE 3 CARBOXYLATE; GALANTAMINE; GLUTARALDEHYDE; ORGANIC SOLVENT; PROPIDIUM IODIDE; RIVASTIGMINE; SCHIFF BASE; SILICON DIOXIDE; TACRINE; UNCLASSIFIED DRUG;

ARTICLE; CAPILLARY ENZYME REACTOR; DRUG POTENCY; DRUG SCREENING; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME REACTOR; IC 50; LIQUID CHROMATOGRAPHY; PRIORITY JOURNAL; REACTION TIME; ULTRAVIOLET SPECTROSCOPY;

ACETYLCHOLINESTERASE; ANIMALS; BIOREACTORS; CALIBRATION; CHOLINESTERASE INHIBITORS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; COUMARINS; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORUS; ENZYME STABILITY; ENZYMES, IMMOBILIZED; HIGH-THROUGHPUT SCREENING ASSAYS; LIGANDS; MOLECULAR STRUCTURE; SILICON DIOXIDE; SURFACE PROPERTIES;

EID: 84869500837     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2012.01.026     Document Type: Article

References (34)

1. Bruhlmann C., Marston A., Hostettmann K., Carrupt P., Testa B. Screening of non-alkaloidal natural compounds as acetylcholinesterase inhibitors. Chem. Biodivers. 2004, 1:819-829.
2. Giacobini E. Cholinesterase inhibitors: from the Calabar bean to Alzheimer therapy. Cholinesterases and Cholinesterase Inhibitors 2000, 181-226. Martin Dunitz, London. E. Giacobini (Ed.).
3. Giacobini E. Cholinesterase and Cholinesterase inhibitors 2000, Martin Dunitz Ltd., London, p. 270.
4. Giacobini E., Pepeu G. The Brain Cholinergic System: In Health and Disease 2006, Informa Healthcare, Oxon.
5. Ellman G.L., Courtney K.D., Andres V., Featherstone M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 1961, 7:88-95.
6. Miao Y.Q., He N.Y., Zhu J.J. History and new developments of assays for cholinesterase activity and inhibition. Chem. Rev. 2010, 110:5216-5234.
7. Ingkaninan K., de Best C.M., Van der Heijden R., Hofte A.J.P., Karabatak B., Irthb H., Tjaden U.R., Van der Greef J., Verpoorte R. High-performance liquid chromatography with on-line coupled UV, mass spectrometric and biochemical detection for identification of acetylcholinesterase inhibitors from natural products. J. Chromatogr. A 2000, 872:61-73.
8. Tang Z., Wang T., Kang J. Immobilized capillary enzyme reactor based on layer-by-layer assembling acetylcholinesterase for inhibitor screening by CE. Electrophoresis 2007, 28:2981-2987.
9. 50) by a direct high-performance liquid chromatographic method on an immobilised acetylcholinesterase column. J. Chromatogr. B: Analyt. Technol. Biomed. Life Sci. 2001, 753:375-383.
10. Cardoso C.L., Lima V.V., Zottis A., Oliva G., Andricopulo A.D., Wainer I.W., Moaddel R., Cass Q.B. Development and characterization of an immobilized enzyme reactor (IMER) based on human glyceraldehyde-3-phosphate dehydrogenase for on-line enzymatic studies. J. Chromatogr. A 2006, 1120:151-157.
11. Markoglou N., Hsuesh R., Wainer I.W. Immobilized enzyme reactors based upon the flavoenzymes monoamine oxidase A and B. J. Chromatogr. B: Biomed. Sci. Appl. 2004, 804:295-302.
12. Boer A.R., Letzel T., van Elswijk D., Lingeman H., Niessen W.M.A., Irth H. On-Line coupling of high-performance liquid chromatography to a continuous-flow enzyme assay based on electrospray ionization mass spectrometry. Anal. Chem. 2004, 76:3155-3161.
13. Forsberg E.M., Gree J.R.A., Brennan J.D. Continuos flow immobilized enzyme reactor-tamdem mass spectrometry for screening of AChE inhibitors in com plex mixtures. Anal. Chem. 2011, 83:5230-5236.
14. Besanger T.R., Hodgson R.J., Guillon D., Brennan J.D. Monolithic membrane-receptor columns: optimization of column performance for frontal affinity chromatography/mass spectrometry applications. Anal. Chim. Acta 2006, 561:107-118.
15. Bonneta C., Andreescub S., Marty J.-L. Adsorption: an easy and efficient immobilisation of acetylcholinesterase on screen-printed electrodes. Anal. Chim. Acta 2003, 481:209-211.
16. Bartolini M., Cavrini V., Andrisano V. Choosing the right chromatographic support in making a new acetylcholinesterase-micro-immobilised enzyme reactor for drug discovery. J. Chromatogr. A 2005, 1065:135-144.
17. Miroslav P., Kamil M., Kamil K. Progress of biosensors based on cholinesterase inhibition. Curr. Med. Chem. 2009, 16:1790-1798.
18. Doong R.-A., Tsai H-C. Immobilization and characterization of sol-gel-encapsulated acetylcholinesterase fiber-optic biosensor. Anal. Chim. Acta 2001, 434:239-246.
19. Vakurova A., Simpsona C.E., Dalya C.L., Gibsonb T.D., Millnera P.A. Acetylcholinesterase-based biosensor electrodes for organophosphate pesticide detection II. Immobilization and stabilization of acetylcholinesterase. Biosens. Bioelectron. 2005, 20:2324-2329.
20. Laschi S., Ogoónczyk D., Palchetti I., Mascini M. Evaluation of pesticide-induced acetylcholinesterase inhibition by means of disposable carbon-modified electrochemical biosensors. Enzyme Microb. Technol. 2007, 40:485-489.
21. Bartolini M.C., Cavrini V., Andrisano V. Monolithic micro-immobilized-enzyme reactor with human recombinant acetylcholinesterase for on-line inhibition studies. J. Chromatogr. A 2004, 1031:27-34.
22. Bartolini M., Cavrini V., Andrisano V. Characterization of reversible and pseudo-irreversible acetylcholinesterase inhibitors by means of an immobilized enzyme reactor. J. Chromatogr. A 2007, 1144:102-110.
23. Gabrovska K., Nedelcheva T., Godjevargova T., Stoilova O., Manolova N., Rashkov I. Immobilization of acetylcholinesterase on new modified acrylonitrile copolymer membranes. J. Mol. Catal. B: Enzym. 2008, 55:169-176.
24. Tümtürk H., Ferat S., Gökhan D. A new method for immobilization of acetylcholinesterase. Bioprocess Biosyst. Eng. 2007, 30.
25. Cardoso C.L., de Moraes M.C., Guido R.V.C., Oliva G., Andricopulo A.D., Wainer I.W., Moaddel R., Cass Q.B. The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi: the effect of species' specific differences on the immobilization. Analyst 2008, 133:93-99.
26. Cassiano N.M., Barreiro J.C., Martins L.R.R., Oliveira R.V., Cass Q.B. Chromatographic methods validation for analysis of small molecules in biological matrices. Quim. Nova 2009, 32:1021-1030.
27. Guidance for Industry-Bioanalytical Method Validation 2001, States Food and Drug Administration (US-FDA).
28. Rhee I.K., van de Meent M., Ingkaninan K., Verpoorte R. Screening for acetylcholinesterase inhibitors from Amaryllidaceae using silica gel thin layer chromatography in combination with bioactivity staining. J. Chromatogr. A 2001, 915:217-223.
29. Alvim J., Dias R.L.A., Castilho M.S., Oliva G., Corrêa A.G. Preparation and evaluation of a coumarin library towards the inhibitory activity of the enzyme gGAPDH from Trypanosoma cruzi. J. Braz. Chem. Soc. 2005, 16:763-773.
30. Vieira L.C.C. Síntese de uma coleção de lignanas e análogo, canditados a fármacos antichagásicos 2010, Chemistry Department, Universidade Federal de São Carlos, São Carlos.
31. Enzymes 1964, Longmans, London, UK. 2nd ed. M. Dixon, E.C. Webb (Eds.).
32. Klibanov A.M. Why are enzymes less active in organic solvents than in water?. TIBTECH 1997, 15:97-101.
33. Plummer J.M., Greenberg M.J., Lehman H.K., Watts J.A. Competitive inhibition by dimethylsulfoxide of molluscan and vertebrate acetylcholinesterase. Biochem. Pharmacol. 1983, 32:151-158.
34. Piazzi L., Cavalli A., Colizzi F., Belluti F., Bartolini M., Mancini F., Recanatini M., Andrisano V., Rampa A. Multi-target-directed coumarin derivatives: hAChE and BACE1 inhibitors as potential anti-Alzheimer compounds. Bioorg. Med. Chem. Lett. 2008, 18:423-426.