Molecular modeling studies on the interactions of aflatoxin B1 and its metabolites with human acetylcholinesterase. Part II: Interactions with the catalytic anionic site (CAS)

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/60162694:G44__/18:43889634

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Molecular modeling studies on the interactions of aflatoxin B1 and its metabolites with human acetylcholinesterase. Part II: Interactions with the catalytic anionic site (CAS)

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Molecular modeling studies on the interactions of aflatoxin B1 and its metabolites with human acetylcholinesterase. Part II: Interactions with the catalytic anionic site (CAS)

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30107 - Medicinal chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Toxins

ISSN

2072-6651

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

11

Strana od-do

1-11

Kód UT WoS článku

000448820400010

EID výsledku v databázi Scopus

2-s2.0-85054136518