Molecular modeling studies on the interactions of aflatoxin B1 and its metabolites with the peripheral anionic site of human acetylcholinesterase

References

• Abraham, M. J., Murtola, T., Schulz, R., Pall, S., Smith, J. C., Hess, B., & Lindahl, E. (2015). High performance molecular simulations through multi-level parallelism from laptops to supercomputers. Software X, 1–2, 19–25. doi: 10.1016/j.softx.2015.06.001.
   Google Scholar
• Ahmed, N., & Singh, U. S. (1984). Effect of aflatoxin B1 on brain serotonin and catecholamines in chickens. Toxicology Letters, 21, 365–367. doi:10.1016/0378-4274(84)90098-5.
   PubMed Web of Science ®Google Scholar
• Alentor, V. A. (1990). Aflatoxin contamination in some Nigerian feeds and feedingstuffs: Highlights of some nutritional, physiopathological and economic implications. Food Chemistry, 37, 145–153. doi:10.1016/0308-8146(90)90088-L.
   Web of Science ®Google Scholar
• Almeida, J. S. F. D., Cuya Guizado, T. R., Guimarães, A. P., Ramalho, T. C., Gonçalves, A. S., de Koning, M. C., & França, T. C. C. (2016). Docking and molecular dynamics studies of peripheral site ligand-oximes as reactivators of sarin-inhibited human acetylcholinesterase. Journal of Biomolecular Structures and Dynamics, 34(12), 2632–2642. doi:10.1080/07391102.2015.1124807.
   PubMed Web of Science ®Google Scholar
• Arduini, F., Errico, I., Amini, A., Micheli, L., Palleschi, G., & Moscone, D. (2007). Enzymatic spectrophotometric method for aflatoxin B detection based on acetylcholinesterase inhibition. Analytical Chemistry, 79, 3409–3415. doi:10.1021/ac061819j.
   PubMed Web of Science ®Google Scholar
• Bennet, J. W., & Klich, M. (2003). Mycotoxins. Clinical Microbiology Reviews, 16(3), 497–516. doi:10.1128/CMR.16.3.497–516.2003.
   PubMed Web of Science ®Google Scholar
• Butler, W. H. (1964). Acute toxicity of aflatoxin B1 in rats. British Journal of Cancer, 18, 756–762.
   PubMed Web of Science ®Google Scholar
• Cheung, J., Rudolph, M. J., Bursthteyn, F., Cassidy, M. S., Gary, E. N., Love, J., … Height, J. J. (2012). Structures of human acetylcholinesterase in complex with pharmacologically important ligands. Journal of Medicinal Chemistry, 55, 10282–10286. doi:10.1021/jm300871x.
   PubMed Web of Science ®Google Scholar
• Cometa, M. F., Lorenzinia, P., Fortunaa, S., Volpea, M. T., Meneguza, A., & Palmeryb, M. (2005). In vitro inhibitory effect of aflatoxin B1 on acetylcholinesterase activity in mouse brain. Toxicology, 206, 125–135. doi:10.1016/j.tox.2004.07.009.
   PubMed Web of Science ®Google Scholar
• Dohnal, V., Wu, Q., & Kuca, K. (2014). Metabolism of aflatoxins: Key enzymes and interindividual as well as interspecies differences. Archives of Toxicology, 88, 1635–1644. doi:10.1007/s00204-014-1312-9.
   PubMed Web of Science ®Google Scholar
• Egnibuke, G. N., & Ikegwuonu, F. I. (1984). Effect of aflatoxicosis on acetylcholinesterase activity in the brain and adenohypophysis of the male rat. Neuroscience Letters, 52, 171–174.
   PubMed Web of Science ®Google Scholar
• Guex, N., & Peitsch, M. C. (1997). Swiss-Model and Swiss Pdb viewer: An environment for comparative protein modeling. Electrophoresis, 18, 2714–2723. doi:10.1002/elps.1150181505.
   PubMed Web of Science ®Google Scholar
• Hansmann, T., Sanson, B., Stojan, J., Weik, M., Marty, J., & Fournier, D. (2009). Kinetic insight into mechanism of cholinesterase inhibition by aflatoxin B1 to develop biosensors. Biosensors and Bioelectronics, 24, 2119–2124. doi:10.1002/elps.1150181505. doi:10.1016/j.bios.2008.11.006.
   PubMed Web of Science ®Google Scholar
• Hathway, D. E. (2000). Toxic action/toxicity. Biological Review, 75, 95–127. doi:10.1111/j.1469-185X.1999.tb00042.x.
   PubMed Web of Science ®Google Scholar
• Hehre, W. J., Deppmeier, B. J., & Klunzinger, P. E. (1999). PC Spartan Pro molecular modeling for desktop. Chemical and Engineering News, 77(17), 2. doi:10.1021/cen-v077n017.p002.
   Google Scholar
• Humphrey, W., Dalke, A., & Schulten, K. (1996). VMD-Visual Molecular Dynamics. Journal of Molecular Graphics, 14, 33–38. doi:10.1016/0263-7855(96)00018-5.
   PubMed Web of Science ®Google Scholar
• Jorgensen, W. L., Maxwell, D. S., & Tirado-Rives, J. (1996). Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. Journal of American Chemical Society, 118, 11225–11236. doi:10.1021/ja9621760.
   Web of Science ®Google Scholar
• Kontoyanni, M., McClellan, L. M., & Sokol, G. S. (2004). Evaluation of docking performance: Comparative data on docking algorithms. Journal of Medicinal Chemistry, 47, 558–565. doi:10.1021/jm0302997.
   PubMed Web of Science ®Google Scholar
• Kumari, R., Kumar, R., & Lynn, A. (2014). g_mmpbsa: A GROMACS tool for high-throughput MM-PBSA calculations. Journal of Chemical Information and Modelling, 54, 1951–1962. doi:10.1021/ci500020m.
   PubMed Web of Science ®Google Scholar
• Pohanka, M. (2013). Cholinesterases in biorecognition and biosensors construction: A review. Analytical Letters, 46, 1849–1868. doi:10.1080/00032719.2013.780240.
   Web of Science ®Google Scholar
• Pohanka, M., Musilek, K., & Kuca, K. (2009). Progress of biosensors based on cholinesterase inhibition. Current Medicinal Chemistry, 16, 1790–1798. doi:10.2174/092986709788186129.
   PubMed Web of Science ®Google Scholar
• Pohanka, M., Musilek, K., & Kuca, K. (2010). Evaluation of aflatoxin B1 – Acetylcholinesterase dissociation kinetic using the amperometric biosensor technology: Prospect for toxicity mechanism. Protein & Peptide Letters, 17, 340–342. doi:10.2174/092986610790780396.
   PubMed Web of Science ®Google Scholar
• Ribeiro, A. A. S. T., Horta, B. A. C., & de Alencastro, R. B. (2008). MKTOP: 489 A program for automatic construction of molecular topologies. Journal of the Brazilian Chemical Society, 19(7), 1433–1435. doi:10.1590/S0103-50532008000700031.
   Web of Science ®Google Scholar
• Rieping, W., Habeck, M., Bardiaux, B., Bernard, A., Malliavin, T. E., & Nilges, M. (2007). ARIA2: Automated NOE assignment and data integration in NMR structure calculation. Bioinformatics, 23, 381–382. doi:10.1093/bioinformatics/btl589.
   PubMed Web of Science ®Google Scholar
• Rocha, G. B., Freire, R. O., Simas, A. M., & Stewart, J. J. P. (2006). RM1: A Reparameterization of AM1 for H, C, N, O, P, S, F, Cl, Br, and I. Journal of Computational Chemistry, 27, 1101–1111. doi:10.1002/jcc.20425.
   PubMed Web of Science ®Google Scholar
• Ryan, N. J., Hogan, G. R., Hayes, A. W., Unger, P. D., & Siraj, M. Y. (1979). Aflatoxin B1: Its role in the etiology of Reye’s syndrome. Pediatrics, 64, 71–75.
   PubMed Web of Science ®Google Scholar
• Sanson, B., Colletier, J., Xu, Y., Lang, P. T., Jiang, H., Silman, I., … Weik, M. (2011). Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations. Protein Science, 20, 1114–1118. doi:10.1002/pro.661.
   PubMed Web of Science ®Google Scholar
• Silva, A. W. S., & Vranken, W. F. (2012). ACPYPE-antechamber python parser interface. BMC Research Notes, 5, 367–374. doi:10.1186/1756-0500-5-367.
   PubMedGoogle Scholar
• Soldatkin, O. O., Burdak, O. S., Sergeyeva, T. A., Arkhypova, V. M., Dzyadevych, S. V., & Soldatkin, A. P. (2013). Acetylcholinesterase-based conductometric biosensor for determination of aflatoxin B1. Sensors and Actuators B: Chemical, 188, 999–1003. doi:10.1016/j.snb.2013.06.107.
   Web of Science ®Google Scholar
• Speijers, G. J., & Speijers, M. H. (2004). Combined toxic effects of mycotoxins. Toxicology Letters, 153(1), 91–98. doi:10.1016/j.toxlet.2004.04.046.
   PubMed Web of Science ®Google Scholar
• Squire, R. A. (1981). Ranking animal carcinogens: A proposed regulatory approach. Science, 214, 877–880. doi:10.1126/science.7302565.
   PubMed Web of Science ®Google Scholar
• Stepurska, K. V., Soldatkin, O. O., Arkhypova, V. M., Soldatkin, A. P., Lagarde, F., Jaffrezic-Renault, N., & Dzyadevych, S. V. (2015). Development of novel enzyme potentiometric biosensor based on pH-sensitive field-effect transistors for aflatoxin B1 analysis in real samples. Talanta, 144, 1079–1084. doi:10.1016/j.talanta.2015.07.068.
   PubMed Web of Science ®Google Scholar
• Thomsen, R., & Christensen, M. H. (2006). MolDock: A new technique for high-accuracy molecular docking. Journal of Medicinal Chemistry, 49, 3315–3321. doi:10.1021/jm051197e.
   PubMed Web of Science ®Google Scholar
• Vranken, W. F., Boucher, W., Stevens, T. J., Vogh, R. H., Pajon, A., Llinas, M., … Laue, E. D. (2005). The CCPN data model for NMR spectroscopy: Development of a software pipeline. Proteins: Structure, Function and Bioinformatics, 59, 687–696. doi:10.1002/prot.20449.
   PubMed Web of Science ®Google Scholar
• Walker, R. C., Crowley, M. F., & Case, D. A. (2008). The implementation of a fast and accurate QM/MM potential method in Amber. Journal of Computational Chemistry, 29, 1019–1031. doi:10.1002/jcc.20857.
   PubMed Web of Science ®Google Scholar
• Wang, J., Wang, W., Kollman, P. A., & Case, D. A. (2006). Automatic atom type and bond type perception in molecular mechanical calculations. Journal of Molecular Graphics and Modelling, 25, 247–260. doi:10.1016/j.jmgm.2005.12.005.
   PubMed Web of Science ®Google Scholar
• Warren, D. (2002). The PyMOL molecular graphics system. San Carlos, CA: DeLano Scientific.
   Google Scholar
• Wu, Q., Jezkova, A., Yuan, Z., Pavlikova, L., Dohnal, V., & Kuca, K. (2009). Biological degradation of aflatoxins. Drug Metabolism Reviews, 41(1), 1–7. doi:10.1080/03602530802563850.
   PubMed Web of Science ®Google Scholar