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    Antiproliferative effects of 5FU-AgNPs on different breast cancer cells
    (Taylor & Francis Ltd, 2024) Danisman-Kalindemirtas, Ferdane; Kariper, I. Afsin; Ustundag, Hilal; Ozsoy, Ceylan; Erdem-Kuruca, Serap
    Breast cancer is a leading cause of cancer-related deaths in women, and researchers are seeking more effective treatments. Nanotechnology offers a promising approach by creating nanocarriers to reduce the side effects of cancer drugs. This study synthesized AgNPs-5FU nanoparticles by binding the anticancer drug 5-fluorouracil (5FU) to a silver nanocarrier, significantly increasing 5FU's cytotoxicity. Characterization using DLS, SEM, UV-Vis, and FTIR confirmed the nanoparticles' properties, with a size of 18-28 nm and a PDI of 0.598. The release of 5FU from AgNPs-5FU was about 70%, demonstrating sustained and controlled release. Cytotoxicity results showed that AgNPs-5FU had an IC50 value of 23.006 in MCF-7 cells and 10.41 in 4T1 cells, making it 2.14 and 4.64 times more effective than free 5FU, respectively. Low cytotoxicity was observed in HUVEC cells. This study indicates that AgNPs-5FU has significantly higher potential activity against cancer cells compared to free 5FU.
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    Pyrazolyl-Benzoxazinone Derivatives as Dual Hsp Inhibitors in Human Breast Cancer
    (Wiley-V C H Verlag Gmbh, 2022) Koca, Irfan; Kamaci, Volkan; Ozsoy, Ceylan; Sert, Yusuf; Kani, Ibrahim; Tutar, Lutfi; Tutar, Yusuf
    Heat Shock Proteins (Hsps) play major role on the onset of several cancers. Metabolic rates of cancer cells are higher compared to that of untransformed cells. This accelerated rate force functional substrate proteins to fold faster than normal folding rate. Although, the process leads cell cycle halting and eventually induces apoptosis, Hsps help cell survival and inhibit apoptosis and fold substrate proteins especially signaling proteins. When cancer cells accelerate the metabolism for invasion and metastasis, substrate proteins must fold to their native state rapidly. Since, functional forms of the proteins must be folded properly, cancer cells overexpress Hsps to fold substrate proteins and avoid apoptosis. Hsp90 and Hsp70 play key role in these processes. Inhibition of either Hsp90 or Hsp70 display complementary function. Therefore, dual inhibition of Hsp70 and Hsp90 potentially provides anticancer affect. In silico studies showed that pyrazolyl-benzoxazine derivatives display binding activity for both Hsps. For this purpose, pyrazole-3-carbonyl chloride were converted to pyrazolyl-benzoxazine derivatives via reactions of anthranilic acids in good yields (68-83 %). The structures of the newly synthesized compounds were elucidated by IR-NMR spectroscopy, elemental analysis, and single-crystal X-ray diffraction. Binding of the compounds inhibit function of Hsps and cause cytotoxic effect over MCF-7 cells. The compounds display potential anticancer effects.