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Toxins 2018, 10(10), 389; https://doi.org/10.3390/toxins10100389

Molecular Modeling Studies on the Interactions of Aflatoxin B1 and Its Metabolites with Human Acetylcholinesterase. Part II: Interactions with the Catalytic Anionic Site (CAS)

1
Laboratory of Molecular Modeling Applied to Chemical and Biological Defense, Military Institute of Engineering, Praca General Tiburcio 80, Rio de Janeiro 22290-270, Brazil
2
Department of Chemistry, Faculty of Science, University of Hradec Kralove, Rokitanskeho 62, 50003 Hradec Kralové, Czech Republic
3
Center for Basic and Applied Research, Faculty of Informatics and Management, University of Hradec Kralove, Rokitanskeho 62, 50003 Hradec Kralové, Czech Republic
4
Department of Toxicology, Faculty of Military Healthy Sciences, University of Defense, Trebesska 1575, 50001 Hradec Kralové, Czech Republic
*
Authors to whom correspondence should be addressed.
Received: 28 July 2018 / Revised: 13 September 2018 / Accepted: 20 September 2018 / Published: 25 September 2018
(This article belongs to the Special Issue Modelling for Risk Assessment of Mycotoxins)
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Abstract

The most common type of aflatoxin (AFT) found in nature is aflatoxin B1 (AFB1). This micotoxin is extremely hepatotoxic and carcinogenic to mammals, with acute and chronic effects. It is believed that this could be related to the capacity of AFB1 and its metabolites in inhibiting the enzyme acetylcholinesterase (AChE). In a previous work, we performed an inedited theoretical investigation on the binding modes of these molecules on the peripheral anionic site (PAS) of human AChE (HssAChE), revealing that the metabolites can also bind in the PAS in the same way as AFB1. Here, we investigated the binding modes of these compounds on the catalytic anionic site (CAS) of HssAChE to compare the affinity of the metabolites for both binding sites as well as verify which is the preferential one. Our results corroborated with experimental studies pointing to AFB1 and its metabolites as mixed-type inhibitors, and pointed to the residues relevant for the stabilization of these compounds on the CAS of HssAChE. View Full-Text
Keywords: aflatoxin B1; metabolites; acetylcholinesterase; catalytic anionic site aflatoxin B1; metabolites; acetylcholinesterase; catalytic anionic site
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de Almeida, J.S.F.D.; Dolezal, R.; Krejcar, O.; Kuca, K.; Musilek, K.; Jun, D.; França, T.C.C. Molecular Modeling Studies on the Interactions of Aflatoxin B1 and Its Metabolites with Human Acetylcholinesterase. Part II: Interactions with the Catalytic Anionic Site (CAS). Toxins 2018, 10, 389.

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