Determination of the gold nanoparticles optimal parameters as a matrix for the immobilization of highly purified human butyrylcholinesterase
Federal State Unitary Enterprise "Research Institute of Hygiene, Toxicology and Occupational Pathology" of Medical and Biological Agency, Russia
Brief summary
The purpose of the work is the use of gold nanoparticles having the optimal configuration as a platform for the immobilization of highly purified butyrylcholinesterase (hpBuChE). The possibilities as a matrix for the immobilization of gold nanoparticles of the following shapes and dimensions were synthesized and studied: nanospheres 15 nm and 50 nm, as well as nanorods 12 × 46 nm and 20 × 60 nm.
The study of the activity of the obtained immobilized forms of highly purified butyrylcholinesterase in in vitro experiments revealed the increase in substrate activity of enzyme conjugates with gold nanospheres of 15.1 nm by 28% compared with the activity of the native enzyme. HpBuChE conjugates with gold nanoparticles with a diameter of 50 nm were less active, but also exceeded the initial form by 8.5%. The use of gold nanorods as a matrix for immobilization led to inhibition of enzyme activity.
2. Sokolov O.I., Selivanov N.U., Selivanova O.G., Velikorodnaya U.I., Dikman L.A., Bogatirev V.A., Pochepcov A.Ya., Filatov B.N. Sravnitelnii analiz Kataliticheskoi aktivnosti visokoochishennoi bytirilholinesterazi cheloveka v nativnoi i konugirovannoi s nanochasticami zolota formah v opitah in vivo / Vestnik Volgogradskogo gosydarstvennogo medicinskogo yniversiteta. 2017. T. 64. ? 4. S. 90-95. doi: 10.19163/1994-9480-2017-4(64)-90-95.
3. Arnida, Janát-Amsbury M.M., Ray A., Peterson C.M., Ghandehari H. Geometry and surface characteristics of gold nanoparticles influence their biodistribution and uptake by macrophages / Eur. J. Pharm. Biopharm. 2011. Vol. 77, N 3. P. 417-423. doi: 10.1016/j.ejpb.2010.11.010.
4. Ding S., Cargill A.A., Medintz I.L., Claussen J.C. Increasing the activity of immobilized enzymes with nanoparticle conjugation / Curr. Opin. Biotechnol. 2015. Vol. 34. P. 242-250. doi: 10.1016/j.copbio.2015.04.005.
5. Doctor B.P., Saxena A. Bioscavengers for the protection of humans against organophosphate toxicity / Chem-Biol. Interact. 2005. Vol. 157-158. P. 167-171. DOI:10.1016/j.cbi.2005.10.024.
6. Ellman G.L., Courtney K.D., Andres V.Jr., Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity / Biochemical. Rharmacology. 1961. Vol. 7. R. 88-95. doi: 10.1016/0006-2952(61)90145-9.
7. Fard J.K., Jafari S., Eghbal M.A. A Review of molecular mechanisms involved in toxicity of nanoparticles / Adv. Pharm. Bull. 2015. Vol. 5, N 4. P. 447-454. doi: 10.15171/apb.2015.061.
8. Gaydess A., Duysen E., Li Y., Gilman V., Kabanov A., Lockridge O., Bronich T. Visualization of exogenous delivery of nanoformulated butyrylcholinesterase to the central nervous system / Chem. Biol. Interact. 2010. Vol. 187. P. 295-298. doi: 10.1016/j.cbi.2010.01.005.
9. Hester K., Liu J., Flynn N., Sultatos L.G., Geng L., Brimijoin S., Ramsey J.D., Hartson S., Ranjan A., Pope C. Polyionic complexes of butyrylcholinesterase and poly-l-lysine-g-poly(ethylene glycol): comparative kinetics of catalysis and inhibition and in vitro inactivation by proteases and heat / Chem. Biol. Interact. 2017. Vol. 275. P. 86-94. doi: 10.1016/j.cbi.2017.07.019.
10. Jana N.R., Gearheart L., Murphy C.J. Wet chemical synthesis of high aspect ratio cylindrical gold nanorods / J. Phys. Chem. B. 2001. Vol. 105, N 19. P. 4065-4067. doi.org/10.1021/jp0107964.
11. Longmire M.R., Ogawa M., Choyke P.L., Kobayashi H. Biologically optimized nanosized molecules and particles: more than just size / Bioconjugate Chem. 2011. Vol. 22. N 6. P. 993-1000. doi: 10.1021/bc200111p.
12. Nelson J.M., Griffin E.G. Adsorption of Invertase / J. Am. Chem. Soc. 1916.Vol. 38. P. 1109-1115. doi: org/10.1021/ja02262a018.
13. Pissuwan D., Niidome T., Cortie M.B. The forthcoming applications of gold nanoparticles in drug and gene delivery systems / J. Control Release. 2011. Vol. 149. P. 65-71. doi: 10.1016/j.jconrel.2009.12.006.
14. Pope C., Uchea C., Flynn N., Poindexter K., Geng L., Brimijoin W.S., Hartson S., Ranjan A., Ramsey J.D., Liu J. In vitro characterization of cationic copolymercomplexed recombinant human butyrylcholinesterase / Biochem. Pharmacol. 2015. Vol. 98. P. 531-539. doi. org/10.1016/j.bcp.2015.10.005.
15. Rahhal T.B., Fromen C.A., Wilson E.M., Kai M.P., Shen T.W., Luft J.C., DeSimone J.M. Pulmonary delivery of butyrylcholinesterase as a model protein to the lung / Mol. Pharmacol. 2016. Vol. 13. P. 1626-1635. doi: 10.1021/acs.molpharmaceut.6b00066.
16. Waiskopf N., Shweky I., Lieberman I., Banin U., Soreq H. Quantum dot labeling of butyrylcholinesterase maintains substrate and inhibitor interactions and cell adherence features / ACS Chem. Neurosci. 2011. Vol. 2. P. 141-150. doi: 10.1021/cn1000827.
17. Wu C-L., Chen Y-P., Yang J-C., Lo H-F., Long L-L. Characterization of lysine-tagged Bacillus stearothermophilus leucine aminopeptidase II immobilized onto carboxylated gold nanoparticles / J. Mol. Catal. B: Enzym. 2008. Vol. 54. R. 83-89. doi: 10.1016/j.molcatb.2007.12.024.
18. Zhang P., Jain P., Tsao C., Sinclair A., Sun F., Hung H.C., Bai T., Wu K., Jiang S. Butyrylcholinesterase nanocapsule as a long circulating bioscavenger with reduced immune response / J. Control. Release. 2016. Vol. 230. P. 73-78. doi: 10.1016/j.jconrel.2016.06.040.