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Alteration of cholinesterase activity as possible mechanism of silver nanoparticle toxicity
Authors:Goran ?inko  Ivana Vinkovi? Vr?ek  Walter Goessler  Gerd Leitinger  Adriana Dijano?i?  Sne?ana Miljani?
Institution:1. Institute for Medical Research and Occupational Health, Ksaverska cesta 2, 10 000, Zagreb, Croatia
2. Institute for Chemistry, Analytical Chemistry, Karl-Franzens University, Stremayrgasse 16/III, 8010, Graz, Austria
3. Institute of Cell Biology, Histology and Embryology, Centre for Molecular Medicine (ZMM), Medical University of Graz, Harrachgasse 21, 8010, Graz, Austria
4. Core Facility Ultrastructure Analysis, Centre for Medical Research (ZMF), Medical University of Graz, Stiftingtalstrasse 24, 8010, Graz, Austria
5. Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102A, 10 000, Zagreb, Croatia
Abstract:Due to their broad-spectrum antimicrobial activity, silver nanoparticles (AgNPs) have been used in a large number of commercial and medical products. Such proliferated AgNP production poses toxicological and environmental issues which need to be addressed. The present study aimed to investigate the effects of AgNPs on acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), important enzymes in areas of neurobiology, toxicology and pharmacology. Three different AgNPs, prepared by the chemical reduction using trisodium citrate, hydroxylamine hydrochloride (Cl-AgNPs), and borohydride following stabilization with poly(vinyl alcohol), were purified and characterised with respect to their sizes, shapes and optical properties. Their inhibition potential on AChE and BChE was evaluated in vitro using an enzyme assay with o-nitrophenyl acetate or o-nitrophenyl butyrate as substrates, respectively. All three studied AgNPs were reversible inhibitors of ChEs. Among tested nanoparticles, Cl-AgNP was found to be the most potent inhibitor of both AChE and BChE. Although the detailed mechanism by which the AgNPs inhibit esterase activities remains unknown, structural perturbation of the enzyme may be the common mode of ChE inhibition by AgNPs.
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