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dc.contributor.authorHill, Katie L.
dc.contributor.authorMortensen, Åse-Karen
dc.contributor.authorTeclechiel, Daniel
dc.contributor.authorWillmore, William G.
dc.contributor.authorSylte, Ingebrigt
dc.contributor.authorJenssen, Bjørn Munro
dc.contributor.authorLetcher, Robert James
dc.date.accessioned2019-08-27T11:23:59Z
dc.date.available2019-08-27T11:23:59Z
dc.date.created2018-06-19T13:25:32Z
dc.date.issued2017
dc.identifier.citationEnvironmental Science and Technology. 2018, 52 (3), 1533-1541.nb_NO
dc.identifier.issn0013-936X
dc.identifier.urihttp://hdl.handle.net/11250/2611190
dc.description.abstractTetradecabromo-1,4-diphenoxybenzene (TeDB-DiPhOBz) is a highly brominated additive flame retardant (FR). Debrominated photodegradates of TeDB-DiPhOBz are hydroxylated in vitro in liver microsomal assays based on herring gulls (Larus argentatus), including one metabolite identified as 4″-OH-2,2′,2″,4-tetrabromo-DiPhOBz. Chemically related methoxylated tetra- to hexabromo-DiPhOBzs are known contaminants in herring gulls. Collectively, nothing is currently known about biological effects of these polybrominated (PB) DiPhOBz-based compounds. The present study investigated the potential thyroidogenicity of 2,2′,2″,4-tetrabromo-(TB)-DiPhOBz along with its para-methoxy (MeO)- and hydroxy-(OH)-analogues, using an in vitro competitive protein binding assay with the human thyroid hormone (TH) transport proteins transthyretin (hTTR) and albumin (hALB). This model para-OH-TB-DiPhOBz was found to be capable of competing with thyroxine (T4) for the binding site on hTTR and hALB. In silico analyses were also conducted using a 3D homology model for gull TTR, to predict whether these TB-DiPhOBz-based compounds may also act as ligands for an avian TH transport protein despite evolutionary differences with hTTR. This analysis found all three TB-DiPhOBz analogues to be potential ligands for gull TTR and have similar binding efficacies to THs. Results indicate structure-related differences in binding affinities of these ligands and suggest there is potential for these contaminants to interact with both mammalian and avian thyroid function.nb_NO
dc.language.isoengnb_NO
dc.publisherAmerican Chemical Societynb_NO
dc.titleIn Vitro and in Silico Competitive Binding of Brominated Polyphenyl Ether Contaminants with Human and Gull Thyroid Hormone Transport Proteinsnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionacceptedVersionnb_NO
dc.source.pagenumber1533-1541nb_NO
dc.source.volume52nb_NO
dc.source.journalEnvironmental Science and Technologynb_NO
dc.source.issue3nb_NO
dc.identifier.doi10.1021/acs.est.7b04617
dc.identifier.cristin1592289
dc.relation.projectNorges forskningsråd: 268419nb_NO
dc.description.localcode© American Chemical Society 2017. This is the authors accepted and refereed manuscript to the article. Locked until 28.12.2018 due to copyright restrictions.nb_NO
cristin.unitcode194,66,10,0
cristin.unitnameInstitutt for biologi
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.fulltextpostprint
cristin.qualitycode2


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