Surface screening, molecular modeling and in vitro studies on the interactions of aflatoxin M1 and human enzymes acetyl- and butyrylcholinesterase

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F19%3A50015658" target="_blank" >RIV/62690094:18470/19:50015658 - isvavai.cz</a>

Alternative codes found

RIV/60162694:G44__/19:00537491 RIV/62690094:18450/19:50015658

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0009279719303357?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0009279719303357?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.cbi.2019.05.022" target="_blank" >10.1016/j.cbi.2019.05.022</a>

Result language

angličtina

Original language name

Surface screening, molecular modeling and in vitro studies on the interactions of aflatoxin M1 and human enzymes acetyl- and butyrylcholinesterase

Original language description

Aflatoxin M1 (AFM1) is a mycotoxin produced by Aspergillus fungi and found in contaminated milk, breastfeed and dairy products, being highly toxic and carcinogenic to humans and other mammalian species. It is also produced in the human body as a metabolite of aflatoxin B1 (AFB1), one of the most toxic natural products known. Previous studies have shown that AFM1 is a potential inhibitor of the enzyme acetylcholinesterase (AChE), and therefore, a potential neurotoxic agent. In this work, surface screening (SS) and molecular dynamics (MD) simulation on human acetylcholinesterase AChE (HssAChE) were performed to corroborate literature data regarding preferential binding sites and type of inhibition. Also, an inedited theoretical study on the interactions of AFM1 with human butyrylcholinesterase (HssBChE) was performed. In vitro inhibition tests on both enzymes were done to support theoretical results. MD simulations suggested the catalytic anionic site of HssAChE as the preferential binding site for AFM1 and also that this metabolite is not a good inhibitor of HssBChE, corroborating previous studies. In vitro assays also corroborated molecular modeling studies by showing that AFM1 did not inhibit BChE and was able to inhibit AChE, although not as much as AFB1.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

30107 - Medicinal chemistry

Project

<a href="/en/project/GA18-01734S" target="_blank" >GA18-01734S: Butyrylcholinesterase reactivators for preparation of pseudo-catalytic scavengers applicable for organophosphorus intoxications</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2019

Confidentiality

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

Name of the periodical

Chemico-biological interactions

ISSN

0009-2797

e-ISSN

—

Volume of the periodical

308

Issue of the periodical within the volume

Aug

Country of publishing house

IE - IRELAND

Number of pages

7

Pages from-to

113-119

UT code for WoS article

000474214200012

EID of the result in the Scopus database

2-s2.0-85066079621