ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013
New tungstenocenes containing 3-hydroxy-4-pyrone ligands: antiproliferative activity on HT-29 and MCF-7 cell lines and binding to human serum albumin studied by fluorescence spectroscopy and molecular modeling methods.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 10 citations in OpenAlex.
- Anticancer Metallocenes and Metal Complexes of Transition Elements from Groups 4 to 7.Molecules (Basel, Switzerland) · 2024Review
- Anticancer Tungstenocenes with a Diverse Set of (Pharmaceutics · 2023Article
- Interaction of metallocene dichlorides with apo-human transferrin: A spectroscopic study and cytotoxic activity against human cancer cell lines.International journal of molecular biology (Edmond, Okla.) · 2020Article
- Crystal structure of 16-ferrocenylmethyl-3β-hydroxy-estra-1,3,5(10)-trien-17-one: a potential chemotherapeutic drug.Acta crystallographica. Section E, Crystallographic communications · 2016Article
- A comparative analysis on the binding characteristics of various mammalian albumins towards a multitherapeutic agent, pinostrobin.Experimental animals · 2015Article
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3 authors at 1 institution in 1 country.
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Abstract
Three new water-soluble tungstenocene derivatives were synthesized and characterized using 3-hydroxy-4-pyrone ligands, which provide aqueous stability to the complexes. The antiproliferative activities of the complexes on HT-29 colon cancer and MCF-7 breast cancer cell lines were evaluated by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay and showed the new tungstenocene derivatives have higher antiproliferative action than tungstenocene dichloride (Cp(2)WCl(2), where Cp is cyclopentadienyl). The binding interactions of the tungstenocenes with human serum albumin (HSA) were investigated using fluorescence spectroscopy and molecular modeling methods. Analysis of the fluorescence quenching spectra indicates that the tungstenocene complexes bind HSA by hydrophobic interactions and hydrogen bonding at fatty acid binding site 6 and drug binding site II. Docking studies provided a description of the hydrophobic interactions and hydrogen bonding by which the tungstenocenes become engaged with HSA. It was determined that the binding affinity of the tungstenoecenes for HSA is in the order Cp(2)WCl(2) < [Cp(2)W(ethyl maltolato)]Cl < [Cp(2)W(maltolato)]Cl < [Cp(2)W(kojato)]Cl, consistent with the hydrophobic interactions and the number of hydrogen bonds involved.
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