• YAN LI

      Articles written in Journal of Chemical Sciences

    • Disposable amperometric immunosensor based on layer-by-layer electro-depositing of the nanogold particles, prussian blue-modified indium tin oxide for determination of 𝛼-fetoprotein

      Yan Li Wen-Bin Liang Li-Chao Fang Hui Huang Jun Deng Jun-Song Zheng

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      In this paper, a novel disposable immunosensor for the detection of 𝛼-fetoprotein (AFP) based on the Indium tin oxide (ITO) modified by the sequential electro-deposition of the nanogold particles (nano-Au) and prussian blue (PB) is described. The ITO is employed to reduce the cost, instead of expensive gold electrode, glassy carbon electrode or platinum electrode. The layer-by-layer (LBL) electro-deposition of the nano-Au, PB is used for blocking the possible leakage from the substrate electrode surface and to prevent shedding of composite membrane. Under optimal conditions, the proposed immunosensor displays a broad linear response to AFP, the working range being 0.25 to 300.0 ng mL-1 with a detection limit of 0.04 ng mL-1. The studied immunosensor exhibits high sensitivity, fast analytical time and good stability. The proposed methodology is potentially attractive for clinical immunoassays.

    • Synthesis, evaluation and in silico studies of novel BRD4 bromodomain inhibitors bearing a benzo[d]isoxazol scaffold

      MAOFENG ZHANG ZHUYUN LIU LIZHONG WANG YAN LI YONGGANG MA

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      The BRD4 protein is associated with various diseases, which has been an attractive target for the treatment of cancer and inflammation. This paper is a follow-up to our previous studies, in which we report the structure-based design, synthesis, and evaluation of a new class of small-molecule BRD4 bromodomain inhibitors bearing a benzo[d]isoxazol scaffold. The SARs focused on exploration of the 2¢ or 3¢ position to afford novel inhibitors that may avoid potential metabolically unstable site. The most potent inhibitor 13f exhibited high binding affinity to BRD4(1) with a DTm value of 7.8 °C as evaluated in thermal shift assay (TSA). The potent activity was also demonstrated by a peptide competition assay with an IC50 value of 0.21 mM. The docking studies revealed the binding mode of the compounds with the active site of BRD4(1). In addition, in silico predictions indicated that these compounds possessed good drug-likeness and pharmacokinetic profile

      This paper is a follow-up to our previous studies, in which we report the structure-based design, synthesis, and evaluation of a new class of small-molecule BRD4 bromodomain inhibitors bearing a benzo[d]isoxazol scaffold.

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