Akademik Veri Yönetim Sistemi
INTERNATIONAL AEGEAN CONFERENCES ON NATURAL & MEDICAL SCIENCES-X, İzmir, Türkiye, 5 - 07 Ekim 2024, ss.312-324
Synthetic pesticides called pyrethroids are used in agricultural, public health, and animal health
to manage insect infestations. Class I pyrethroids (C1Ps), such as permethrin and tetramethrin
share the basic structure of the carboxylic ester cyclopropane. Class II pyrethroids (C2Ps) such
as cyhalothrin, deltamethrin, and cypermethrin, have a cyano group. Worldwide reports of
widespread exposure to pyrethroid insecticides have been made by the general public. It is yet
unknown what effects prolonged pyrethroid exposure may have on oxidative stress and other
long-term human health repercussions. Glutathione S transferases (GSTs) are crucial enzymes
in the metabolism of cellular detoxification of medications, insecticides, and other chemical
compounds. GST Pi (GSTP), one of these enzymes, catalyses the reaction between GSH and
its electrophilic substrates. In this work, in silico techniques were used to examine the inhibitory
effects of five distinct pyrethroids from two families on the human GSTP enzyme. After the
absorption path of these substances was predicted with SwissADME, molecular docking
analyzes were completed with AutoDockTools-1.5.6, UCSF Chimera 1.15, ChimeraX 1.2.5,
Discovery Studio 2021 Client, Maestro 14.0 and CBDock2 software. C1Ps were found to bind
more firmly to the GSTP active site by comparing the binding energies. It was discovered that
the range for C1Ps was -8.1 - -8.4 kcal/mol and for C2Ps it was -7.2 - -7.6 kcal/mol. Permethrin
and tetramethrin bond to the active site amino acids PHE8, VAL10, ILE104, TYR108, and
GLY205. They also form weak interactions with TYR7 and ARG13. Cyhalothrin, deltamethrin,
and cypermethrin similarly form hydrophobic contact and hydrogen bonds with TYR7 and
ARG13. There were, however, comparatively less bonds to the total number of amino acids in
the active site. The pyrethroids that were examined all bound to roughly the same area, but at
varied strengths, and as a result, all of them significantly inhibited GSTP.