dc.contributor.author | Hill, Katie L. | |
dc.contributor.author | Mortensen, Åse-Karen | |
dc.contributor.author | Teclechiel, Daniel | |
dc.contributor.author | Willmore, William G. | |
dc.contributor.author | Sylte, Ingebrigt | |
dc.contributor.author | Jenssen, Bjørn Munro | |
dc.contributor.author | Letcher, Robert James | |
dc.date.accessioned | 2019-08-27T11:23:59Z | |
dc.date.available | 2019-08-27T11:23:59Z | |
dc.date.created | 2018-06-19T13:25:32Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Environmental Science and Technology. 2018, 52 (3), 1533-1541. | nb_NO |
dc.identifier.issn | 0013-936X | |
dc.identifier.uri | http://hdl.handle.net/11250/2611190 | |
dc.description.abstract | Tetradecabromo-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.iso | eng | nb_NO |
dc.publisher | American Chemical Society | nb_NO |
dc.title | In Vitro and in Silico Competitive Binding of Brominated Polyphenyl Ether Contaminants with Human and Gull Thyroid Hormone Transport Proteins | nb_NO |
dc.type | Journal article | nb_NO |
dc.type | Peer reviewed | nb_NO |
dc.description.version | acceptedVersion | nb_NO |
dc.source.pagenumber | 1533-1541 | nb_NO |
dc.source.volume | 52 | nb_NO |
dc.source.journal | Environmental Science and Technology | nb_NO |
dc.source.issue | 3 | nb_NO |
dc.identifier.doi | 10.1021/acs.est.7b04617 | |
dc.identifier.cristin | 1592289 | |
dc.relation.project | Norges forskningsråd: 268419 | nb_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.unitcode | 194,66,10,0 | |
cristin.unitname | Institutt for biologi | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.fulltext | postprint | |
cristin.qualitycode | 2 | |