Analysis of the activation of acetylcholinesterase by carbon nanoparticles using a monolithic immobilized enzyme microreactor: role of the water molecules in the active site gorge

References

• Iijima S. Helical, microtubules of graphitic carbon. Nature 1991;354:56–58.
   Web of Science ®Google Scholar
• Lin Y, Taylor S, Li H, Fernando KAS, Qu L, Wang W, Gu L, Zhou B, Sun YP. Advances toward bioapplications of carbon nanotubes. J Mat Chem. 14; 2004: 527–541.
   Web of Science ®Google Scholar
• Hu C, Hu H. Carbon nanotube-based electrochemical sensors: principles and applications in biomedical systems. J Sensor. 2009, ID 187615, 40 pages.
   Google Scholar
• André C, Agiovlasileti D, Guillaume YC. Peculiarities of a novel bioenzymatic reactor using carbon nanotubes as enzyme activity enhancers: application to arginase. Talanta 2011;85:2703–2706.
   PubMed Web of Science ®Google Scholar
• Pohanka M, Jun D, Kalasz H, Kuca K. Cholinesterase biosensor construction - a review. Protein Pept Lett 2008;15:795–798.
   PubMed Web of Science ®Google Scholar
• Bucur B, Fournier D, Danet A, Marty JL. Biosensors based on highly sensitive acetylcholinesterases for enhanced carbamate insecticides detection. Analytica Chimica Acta 2006;562:115–121.
   Web of Science ®Google Scholar
• Kok FN, Hasirci V. Determination of binary pesticide mixtures by an acetylcholinesterase - choline oxidase biosensor. Biosensors & Bioelectronics 2004;19:661–665.
   PubMed Web of Science ®Google Scholar
• He P, Davies J, Greenway G, Haswell SJ. Measurement of acetylcholinesterase inhibition using bienzymes immobilized monolith micro-reactor with integrated electrochemical detection. Anal Chim Acta 2010;659:9–14.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Ibrahim F, Guillaume YC, Thomassin M, André C. Magnesium effect on the acetylcholinesterase inhibition mechanism: a molecular chromatographic approach. Talanta 2009;79:804–809.
   PubMed Web of Science ®Google Scholar
• Bartolini M, 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.
   PubMed Web of Science ®Google Scholar
• Ellman GL, Courtney KD, Andres V Jr, Feather-Stone RM. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 1961;7:88–95.
   PubMed Web of Science ®Google Scholar
• Copeland RA. Enzymes. A practical introduction to structure, mechanism, and data analysis, Second ed. Analyt Biochem 2001;291:172.
   Google Scholar
• Schallreuter KU, Elwary SM, Gibbons NC, Rokos H, Wood JM. Activation/deactivation of acetylcholinesterase by H2O2: more evidence for oxidative stress in vitiligo. Biochem Biophys Res Commun 2004;315:502–508.
   PubMed Web of Science ®Google Scholar
• Yang M, Zhang J, Zhu KY, Xuan T, Liu X, Guo Y, Ma E. Increased activity and reduced sensitivity of acetylcholinesterase associated with malathion resistance in a field population of the oriental migratory locust, Locusta migratoria manilensis (Meyen). Pesticide Biochemistry and Physiology 2008;91:32–38.
   Web of Science ®Google Scholar
• André C, Ibrahim F, Gharbi T, Herlem G, Guillaume YC. Experimental studies of OH° radical/pressure dependence of arginase activity using a molecular chromatography approach. J Chromatogr B Analyt Technol Biomed Life Sci 2010;878:2826–2830.
   PubMed Web of Science ®Google Scholar
• Bustos-Jaimes I, Mora-Lugo R, Calcagno ML, Farrés A. Kinetic studies of Gly28:Ser mutant form of Bacillus pumilus lipase: changes in k(cat) and thermal dependence. Biochim Biophys Acta 2010;1804:2222–2227.
   PubMed Web of Science ®Google Scholar
• Rosenberry TL, Rabl CR, Neumann E. Binding of the neurotoxin fasciculin 2 to the acetylcholinesterase peripheral site drastically reduces the association and dissociation rate constants for N-methylacridinium binding to the active site. Biochemistry 1996;35:685–690.
   PubMed Web of Science ®Google Scholar
• De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC. A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry 2001;40:10447–10457.
   PubMed Web of Science ®Google Scholar
• Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc Nat Acad Sci 1993;90:9031–9035.
   PubMed Web of Science ®Google Scholar
• Ranaei-Siadat SO, Riazi GH, Sadeghi M, Chang LS, Lin SR, Eghtesadi-Araghi P et al. Modification of substrate inhibition of synaptosomal acetylcholinesterase by cardiotoxins. J Biochem Mol Biol 2004;37:330–338.
   PubMedGoogle Scholar
• Yuyang L, Xianqiong Chen JHX, Xin JH. Super-hydrophobic surfaces from a simple coating method: a bionic nanoengineering approach. Nanotechnology 2006;17: 3259–3265.
   Web of Science ®Google Scholar
• Low PS, Bada JL, Somero GN. Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation. Proc Nat Acad Sci 1973;70:430–432.
   PubMed Web of Science ®Google Scholar
• Loftfield RB, Eigner EA, Pastuszyn A, Lovgren TN, Jakubowski H. Conformational changes during enzyme catalysis: role of water in the transition state. Proc Nat Acad Sci 1980;77:3374–3378.
   PubMed Web of Science ®Google Scholar
• Koellner G, Kryger G, Millard CB, Silman I, Sussman JL, Steiner T. Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica. J Mol Biol 2000;296:713–735.
   PubMed Web of Science ®Google Scholar
• Henchman RH, Tai K, Shen T, McCammon JA. Properties of water molecules in the active site gorge of acetylcholinesterase from computer simulation. Biophys J 2002;82:2671–2682.
   PubMed Web of Science ®Google Scholar