{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nogara PA"],"funding":["CAPES/PrInt – Projeto Institucional de Internacionalização","FAPERGS","CAPES/PROEX","National Council for Scientific and Technological Development","Foundation for Research Support"],"pagination":["100127"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7280828"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15"],"pubmed_abstract":["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>Drosoph"],"journal":["Computational toxicology (Amsterdam, Netherlands)"],"pubmed_title":["The Se<sup>…</sup>S/N interactions as a possible mechanism of δ-aminolevulinic acid dehydratase enzyme inhibition by organoselenium compounds: A computational study."],"pmcid":["PMC7280828"],"funding_grant_id":["°0737/2018","182123/2018-01","005848/2018-31","°88882","374997/2019-00","HP10CUVVQU","° 23038"],"pubmed_authors":["Nogara PA","Orian L","Rocha JBT"],"additional_accession":[]},"is_claimable":false,"name":"The Se<sup>…</sup>S/N interactions as a possible mechanism of δ-aminolevulinic acid dehydratase enzyme inhibition by organoselenium compounds: A computational study.","description":"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>Drosoph","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Aug","modification":"2026-05-02T01:19:09.363Z","creation":"2020-06-27T07:25:52Z"},"accession":"S-EPMC7280828","cross_references":{"pubmed":["32572387"],"doi":["10.1016/j.comtox.2020.100127"]}}