Molecular modeling studies on the interactions of aflatoxin B1 and its metabolites with human acetylcholinesterase. Part II: Interactions with the catalytic anionic site (CAS)
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F18%3A50014699" target="_blank" >RIV/62690094:18470/18:50014699 - isvavai.cz</a>
Alternative codes found
RIV/60162694:G44__/18:43889634
Result on the web
<a href="https://www.mdpi.com/2072-6651/10/10/389" target="_blank" >https://www.mdpi.com/2072-6651/10/10/389</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/toxins10100389" target="_blank" >10.3390/toxins10100389</a>
Alternative languages
Result language
angličtina
Original language name
Molecular modeling studies on the interactions of aflatoxin B1 and its metabolites with human acetylcholinesterase. Part II: Interactions with the catalytic anionic site (CAS)
Original language description
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. © 2018 by the authors.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30107 - Medicinal chemistry
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Toxins
ISSN
2072-6651
e-ISSN
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Volume of the periodical
10
Issue of the periodical within the volume
10
Country of publishing house
CH - SWITZERLAND
Number of pages
11
Pages from-to
1-11
UT code for WoS article
000448820400010
EID of the result in the Scopus database
2-s2.0-85054136518