biostudies-literatureNogara PACAPES/PrInt – Projeto Institucional de InternacionalizaçãoFAPERGSCAPES/PROEXNational Council for Scientific and Technological DevelopmentFoundation for Research Support100127https://www.ebi.ac.uk/biostudies/studies/S-EPMC7280828biostudies-literatureUnknown15Organoselenium compounds present many pharmacological properties and are promising drugs. However, toxicological effects associated with inhibition of thiol-containing enzymes, such as the δ-aminolevulinic acid dehydratase (δ-AlaD), have been described. The molecular mechanism(s) by which they inhibit thiol-containing enzymes at the atomic level, is still not well known. The use of computational methods to understand the physical-chemical properties and biological activity of chemicals is essential to the rational design of new drugs. In this work, we propose an <i>in silico</i> study to understand the δ-AlaD inhibition mechanism by diphenyl diselenide (DPDS) and its putative metabolite, phenylseleninic acid (PSA), using δ-AlaD enzymes from <i>Homo sapiens</i> (<i>Hs</i>δ-AlaD), <i>DrosophComputational toxicology (Amsterdam, Netherlands)The Se^…S/N interactions as a possible mechanism of δ-aminolevulinic acid dehydratase enzyme inhibition by organoselenium compounds: A computational study.PMC7280828°0737/2018182123/2018-01005848/2018-31°88882374997/2019-00HP10CUVVQU° 23038Nogara PAOrian LRocha JBTfalseThe Se^…S/N interactions as a possible mechanism of δ-aminolevulinic acid dehydratase enzyme inhibition by organoselenium compounds: A computational study.Organoselenium compounds present many pharmacological properties and are promising drugs. However, toxicological effects associated with inhibition of thiol-containing enzymes, such as the δ-aminolevulinic acid dehydratase (δ-AlaD), have been described. The molecular mechanism(s) by which they inhibit thiol-containing enzymes at the atomic level, is still not well known. The use of computational methods to understand the physical-chemical properties and biological activity of chemicals is essential to the rational design of new drugs. In this work, we propose an <i>in silico</i> study to understand the δ-AlaD inhibition mechanism by diphenyl diselenide (DPDS) and its putative metabolite, phenylseleninic acid (PSA), using δ-AlaD enzymes from <i>Homo sapiens</i> (<i>Hs</i>δ-AlaD), <i>Drosoph2020-01-01T00:00:00Z2020 Aug2026-05-02T01:19:09.363Z2020-06-27T07:25:52ZS-EPMC72808283257238710.1016/j.comtox.2020.100127