Synthesis, characterization and biological studies of new antimony(III) halide complexes with omega-thiocaprolactam

dc.contributor.authorOzturk, IIen
dc.contributor.authorBanti, C. N.en
dc.contributor.authorManos, M. J.en
dc.contributor.authorTasiopoulos, A. J.en
dc.contributor.authorKourkoumelis, N.en
dc.contributor.authorCharalabopoulos, K.en
dc.contributor.authorHadjikakou, S. K.en
dc.date.accessioned2015-11-24T19:43:26Z
dc.date.available2015-11-24T19:43:26Z
dc.identifier.issn1873-3344-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24756
dc.rightsDefault Licence-
dc.titleSynthesis, characterization and biological studies of new antimony(III) halide complexes with omega-thiocaprolactamen
heal.abstractThree new antimony(III) halide complexes (SbX(3), X=Cl, Br and I) with the heterocyclic thione omega-thiocaprolactam (1-azacycloheptane-2-thione, (Hthcl)) of formulae {[SbCl(2)(mu(2)-Cl)(Hthcl)(2)](n)} (1), {[(SbBr(2)(mu(2)-Br)(Hthcl)(2))(2)]} (2) and {[(SbI(2)(mu(2)-I)(Hthcl)(2))(2)]} (3) were synthesized from the reaction of antimony(III) halides with omega-thiocaprolactam in 1:2 stoichiometry. The complexes were characterized by elemental analysis, FT-IR spectroscopy, (1)H, (13)C NMR spectroscopy and Thermal Gravimetry-Differential Thermal Analysis (TG-DTA). Crystal structures of the ligand omega-thiocaprolactam and its complexes 1-3 were determined with single crystal X-ray diffraction analysis. Complexes 1-3 and omega-thiocaprolactam were evaluated for their in vitro cytotoxic activity against leiomyosarcoma (LMS) and human breast adenocarcinoma (MCF-7) tumor cell lines. Antimony complexes 1-3 exhibit strong antiproliferative activity against both cell lines tested. The higher such activity was found for 3 with IC(50) values of 0.12+/-0.04muM (LMS) and 0.76+/-0.16muM (MCF-7) which are 60 and 10 times respectively, stronger than that of cisplatin. The influence of these complexes 1-3 and omega-thiocaprolactam upon the catalytic peroxidation of linoleic acid to hyperoxolinoleic acid by the enzyme lipoxygenase (LOX) was kinetically and theoretically studied. The results were shown negligible inhibitory activity of 1-3 against LOX.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1016/j.jinorgbio.2012.01.014-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/22377717-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0162013412000414/1-s2.0-S0162013412000414-main.pdf?_tid=c097bf22c94de0858f57ddf38a0c13aa&acdnat=1333449149_beeb4ef2a49bcde9bc188afa68c33741-
heal.journalNameJ Inorg Biochemen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2012-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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