Adsorption and inhibition of butyrylcholinesterase by different engineered nanoparticles

Chemosphere

Volumn 79, Issue 1, 2010, Pages 86-92

  Wang, Zhenyu ^a   Zhang, Kai ^a   Zhao, Jian ^a,b   Liu, Xiaoyun ^a   Xing, Baoshan ^a,b  

^a OCEAN UNIVERSITY OF CHINA   (China)

^b UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

Biomarker; Butyrylcholinesterase; Carbon nanotubes; Dissolved metal ions; Enzyme; Neurotoxicity

Indexed keywords

ACTIVATED ALUMINA; ACTIVATED CARBON; ADSORPTION; ALUMINUM OXIDE; BIOMARKERS; CARBON NANOTUBES; DISSOLUTION; ENZYMES; MAMMALS; METAL IONS; MULTIWALLED CARBON NANOTUBES (MWCN); NANOPARTICLES; NANOTUBES; SILICA; TITANIUM DIOXIDE;

ALL METAL; BUTYRYLCHOLINESTERASE; DISSOLVED METAL IONS; ENGINEERED NANOPARTICLES; HUMAN SERUM; INHIBITION RATE; INHIBITORY CONCENTRATION; NEUROTOXICITY;

COPPER;

ACTIVATED CARBON; ALUMINUM; ALUMINUM HYDROXIDE; ALUMINUM NANOPARTICLE; CARBON NANOTUBE; CHOLINESTERASE; COPPER ION; METAL NANOPARTICLE; SILICON DIOXIDE; TITANIUM DIOXIDE; UNCLASSIFIED DRUG;

ACTIVATED CARBON; ADSORPTION; BIOMARKER; DISSOLUTION; ENZYME; INHIBITION; NERVOUS SYSTEM; SERUM;

ADSORPTION KINETICS; ARTICLE; CHEMICAL ANALYSIS; CHEMICAL INTERACTION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME INHIBITION; IC 50; NANOANALYSIS; NANOENGINEERING; NEUROTOXICITY;

MAMMALIA;

EID: 77249116243     PISSN: 00456535     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemosphere.2009.12.051     Document Type: Article

References (36)

1. 2 to microalgae Pseudokirchneriella subcapitata. Sci. Total Environ. 407 (2009) 1461-1468
2. Aurbek N., Thiermann H., Eyer F., Eyer P., and Worek F. Suitability of human butyrylcholinesterase as therapeutic marker and pseudo catalytic scavenger in organophosphate poisoning: a kinetic analysis. Toxicology 259 (2009) 133-139
3. Bazilevsky A.V., Sun K., Yarin A.L., and Megaridis C.M. Room-temperature, open-air, wet intercalation of liquids, surfactants, polymers and nanoparticles within nanotubes and microchannels. J. Mater. Chem. 18 (2008) 696-702
4. Bower C.K., Sananikone S., Bothwell M.K., and McGuire J. Activity losses among T4 lysozyme variants after adsorption to colloidal silica. Biotechnol. Bioeng. 64 (1999) 373-376
5. Chilukuri N., Duysen E.G., Parikh K., Sun W., Doctor B.P., Lockridge O., and Saxena A. Adenovirus-mediated gene transfer of human butyrylcholinesterase results in persistent high-level transgene expression in vivo. Chem. Biol. Interact. 175 (2008) 327-331
6. Chou C.C., Hsiao H.Y., Hong Q.S., Chen C.H., Peng Y.W., Chen H.W., and Yang P.C. Single-walled carbon nanotubes can induce pulmonary injury in mouse model. Nano Lett. 8 (2008) 437-445
7. Chuiko G.M. Comparative study of acetylcholinesterase and butyrylcholinesterase in brain and serum of several freshwater fish: specific activities and in vitro inhibition by DDVP, an organophosphorus pesticide. Comp. Biochem. Physiol. Part C 127 (2000) 233-242
8. Ellman G.L., Courtney K.D., Andres V., and Feather-stone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7 (1961) 88-95
9. Grassian V.H. When size really matters: size-dependent properties and surface chemistry of metal and metal oxide nanoparticles in gas and liquid phase environments. J. Phys. Chem. C 112 (2008) 18303-18313
10. Hansen S.F., Michelson E.S., Kamper A., Borling P., Stuer-Lauridsen F., and Baun A. Categorization framework to aid exposure assessment of nanomaterials in consumer products. Ecotoxicology 17 (2008) 438-447
11. Huang Y.J., Huang Y., Baldassarre H., Wang B., Lazaris A., Leduc M., Bilodeau A.S., Bellemare A., Côté M., Herskovits P., Touati M., Turcotte C., Valeanu L., Lemée N., Wilgus H., Bégin I., Bhatia B., Rao K., Neveu N., Brochu E., Pierson J., Hockley D.K., Cerasoli D.M., Lenz D.E., Karatzas C.N., and Langermann S. Recombinant human butyrylcholinesterase from milk of transgenic animals to protect against organophosphate poisoning. Proc. Natl. Acad. Sci. USA 104 (2007) 13603-13608
12. Jiang W., Mashayekhi H., and Xing B. Bacterial toxicity comparison between nano- and micro-scaled oxide particles. Environ. Pollut. 157 (2009) 1619-1625
13. Karlsson H.L., Gustafsson J., Cronholm P., and Möller L. Size-dependent toxicity of metal oxide particles-a comparison between nano- and micrometer size. Toxicol. Lett. 188 (2009) 112-118
14. Kashiwada S. Distribution of nanoparticles in the see-through medaka (Oryzias latipes). Environ. Health Perspect. 14 (2006) 1697-1702
15. 2 with human serum albumin: a fluorescence quenching study. Colloids Surf. A: Physicochem. Eng. Aspects 333 (2009) 91-95
16. King-Heiden T.C., Wiecinski P.N., Mangham A.N., Metz K.M., Nesbit D., Pedersen J.A., Hamers R.J., Heideman W., and Peterson R.E. Quantum dot nanotoxicity assessment using the zebrafish embryo. Environ. Sci. Technol. 43 (2009) 1605-1611
17. Leticia A.G., and Gerardo G.B. Determination of esterase activity and characterization of cholinesterases in the reef fish Haemulon plumieri. Ecotoxicol. Environ. Saf. 71 (2008) 787-797
18. Li B., Stribley J.A., Ticu A., Xie W.H., Schopfer L.M., Hammond P., Brimijoin S., Hinrichs S.H., and Lockridge O. Abundant tissue butyrylcholinesterase and its possible function in the acetylcholinesterase knockout mouse. J. Neurochem. 75 (2000) 1320-1331
19. Liao C.M., Chiang Y.H., and Chio C.P. Assessing the airborne titanium dioxide nanoparticle-related exposure hazard at workplace. J. Hazard. Mater. 162 (2009) 57-65
20. Lynch I., and Dawson K.A. Protein-nanoparticle interactions. Nano Today 3 (2008) 40-47
21. Medina C., Santos-Martinez M.J., Radomski A., Corrigan O.I., and Radomski M.W. Nanoparticles: pharmacological and toxicological significance. Br. J. Pharmacol. 150 (2007) 552-558
22. Patočka J., Cabal J., Kuča K., and Jun D. Oxime reactivation of acetylcholinesterase inhibited by toxic phosphorus esters: in vitro kinetics and thermodynamics. J. Appl. Biomed. 3 (2005) 91-99
23. 3+: comparison of the effects of metal ions on cholinesterases. Comp. Biochem. Physiol. Part C 122 (1999) 181-190
24. Saxena A., Redman A.M.G., Jiang X., Lockridge O., and Doctor B.P. Differences in active-site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase. Chem. Biol. Interact. 119-120 (1999) 61-69
25. Stefano B., Ilaria C., and Silvano F. Cholinesterase activities in the scallop Pecten jacobaeus: characterization and effects of exposure to aquatic contaminants. Sci. Total Environ. 392 (2008) 99-109
26. Suárez D., Díaz N., Fontecilla-Camps J., and Field M.J. A computational study of the deacylation mechanism of human butyrylcholinesterase. Biochemistry 45 (2006) 7529-7543
27. Sun J., and Lynn B.C. Development of a MALDI-TOF-MS method to identify and quantify butyrylcholinesterase inhibition resulting from exposure to organophosphate and carbamate pesticides. J. Am. Soc. Mass Spectrom. 18 (2007) 698-706
28. Vertegel A.A., Siegel R.W., and Dordick J.S. Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme. Langmuir 20 (2004) 6800-6807
29. 2 nanoparticles in the anatase and rutile crystal phases. Toxicol. Lett. 183 (2008) 72-80
30. 2 nanoparticles. Toxicology 254 (2008) 82-90
31. 2 and bovine hemoglobin using spectral methods. Colloids Surf. B 65 (2008) 190-196
32. 2 to the nematode Caenorhabditis elegans. Environ. Pollut. 157 (2009) 1171-1177
33. Wang Z.Y., Zhao J., Li F.M., Gao D.M., and Xing B.S. Adsorption and inhibition of acetylcholinesterase by different nanoparticles. Chemosphere 77 (2009) 67-73
34. Wu X.Y., and Narsimhan G. Effect of surface concentration on secondary and tertiary conformational changes of lysozyme adsorbed on silica nanoparticles. Biochim. Biophys. Acta 1784 (2008) 1694-1701
35. Wu X.Y., and Narsimhan G. Characterization of secondary and tertiary conformational changes of β-lactoglobulin adsorbed on silica nanoparticle surfaces. Langmuir 24 (2008) 4989-4998
36. Yang K., and Xing B.S. Desorption of polycyclic aromatic hydrocarbons from carbon nanomaterials in water. Environ. Pollut. 145 (2007) 529-537