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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Corban, G. J. | en |
| dc.contributor.author | Hadjikakou, S. K. | en |
| dc.contributor.author | Tsipis, A. C. | en |
| dc.contributor.author | Kubicki, M. | en |
| dc.contributor.author | Bakas, T. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.date.accessioned | 2015-11-24T16:40:00Z | - |
| dc.date.available | 2015-11-24T16:40:00Z | - |
| dc.identifier.issn | 1144-0546 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8217 | - |
| dc.rights | Default Licence | - |
| dc.subject | thyroid-hormone synthesis | en |
| dc.subject | x-ray characterization | en |
| dc.subject | i iodothyronine deiodinase | en |
| dc.subject | structural-characterization | en |
| dc.subject | heterocyclic thioamides | en |
| dc.subject | hydrogen-peroxide | en |
| dc.subject | diiodine adducts | en |
| dc.subject | lactoperoxidase | en |
| dc.subject | mechanism | en |
| dc.subject | drugs | en |
| dc.title | Inhibition of peroxidase-catalyzed iodination by thioamides: experimental and theoretical study of the antithyroid activity of thioamides | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1039/C0nj00626b | - |
| heal.identifier.secondary | <Go to ISI>://000285515400031 | - |
| heal.identifier.secondary | http://pubs.rsc.org/en/content/articlepdf/2011/nj/c0nj00626b | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2011 | - |
| heal.abstract | The reaction of di-iodine with N-methyl-2-mercapto-benzothiazole (NMBZT) in the presence of ferric tetra-phenyl-porphyrin chloride (FeTPPCl) in 6 : 3 : 1 (I(2) : thioamide : FeTPPCl) molar ratio yields a mixture of products consisting of the iodonium {[(NMBZT)(2)I](+)center dot[(I(7))(-)]}(n) salt, 1, and the FeTPPCl complex, 2. The compounds were characterized by X-ray diffraction analysis. The crystal structure of 1 was identical to the one already published, while of compound 2 at 294(1) K re-evaluates previous work on it. The inhibition activity of the thioamide ligands (N-methyl-2-mercapto-benzothiazole (NMBZT), 2-mercapto-benzothiazole (MBZT), 5-chloro-2-mercapto benzothiazole (CMBZT), 2-mercaptothiazolidine (MTZT), 2-mercaptopyridine (PySH), thiourea (TU), 1,3-bis(3-pyridyl-methyl)-2-thiourea (PyTU), 2-mercapto-3,4,5,6-tetrahydropyrimidine (THP), 2-mercaptopyrimidine (PmSH), 6-propyl-2-thiouracil (PTU), 6-methyl-2-thiouracil (MTU), di-thiouracil-2,4 (DTUC), 2-mercapto-4-methyl-pyrimidine hydro chloride (MPmCl), methimazole (MMI), 2-mercapto-benzimidazole (BZIM), 5-nitro-2-mercapto-benzimidazole (NiMBZIM), 5-methyl-2-mercapto-benzimidazole (MBZIM), 2-hydroxy-pyrimidine (PmOH), 2-hydroxypyridine (PyOH)) against the catalytic oxidation of iodides by H(2)O(2) in the presence of FeTPPCl (a model of the active site of Thyroid Peroxidase (TPO)) was measured as a result of the yield of I(3)(-) resulting from the oxidation of I(-) and was also evaluated theoretically using electronic structure calculation methods (DFT). The compounds exhibiting high and intermediate degree of inhibition (between 27% and 17%) are MBZT, MMI, PySH, NMBZT, PmSH, MBZIM, NiBZIM and MTZT. The kinetic study of inhibition of lactoperoxidase (LPO) (a model of TPO) is based on the assessment of LPO activity in the presence of its inhibitors-the thioamide compounds. LPO activity can be assayed by measuring guaiacol (gua) peroxidation to tetraguaiacol in the presence of H(2)O(2). The results illustrated that the lowest IC(50) values (<10 mu M) required for the LPO inhibition were exhibited by DTUC, NiMBZIM, MBZT, PySH thioamides. Low concentrations between 10 and 30 mu M are obtained in the case of CMBZT, BZIM, MPmCl, PmSH, MBZIM, and MMI. DFT calculations of the geometric and energetic profiles threw light on the mechanism of the inhibition process by the thioamide compounds scrutinizing all crucial reaction steps and are in agreement with the experimental results. | en |
| heal.publisher | Royal Society of Chemistry | en |
| heal.journalName | New Journal of Chemistry | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Corban-2011-Inhibition of peroxi.pdf | 2.1 MB | Adobe PDF | View/Open Request a copy |
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