• NAYIM SEPAY

      Articles written in Journal of Chemical Sciences

    • Novel chalcones as Bcl-2 inhibitor in lung cancer: docking, design and synthesis of 2,3-Tetrasubstituted-2,3-dihydrobenzofuran-3- carboxamides

      SANKAR P DEY NAYIM SEPAY ASOK K MALLIK AMARENDRA PATRA

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      Some of the chalcones and flavones are very efficient to facilitate the signal of death to the lung cancer cell through blocking the active site BH3 of Bcl-2 proteins. We designed a number of novel chalcones and flavones targeting the active site of the protein. Docking study showed that the designed compounds were very efficient as the reported compounds. We synthesized and characterized some of the designed compounds.2,3-Tetrasubstituted-2,3-dihydrobenzofuran-3-carboxamides were generated as novel products bybase-catalyzed condensation of o-hydroxyacetophenones and p-nitrobenzaldehyde in different alcohols. Detailed NMR spectroscopic analysis including COSY, homodecoupling and HETCOR (one bond as well aslong-range) studies established the structure of the compounds. Mechanistic paths have been suggested for the formation of the novel products.

    • Antioxidant ferulic acid prevents the aggregation of bovine b-lactoglobulin in vitro

      SAMPA PAL SANHITA MAITY SUBRATA SARDAR SHAHNAZ BEGUM RAMKRISHNA DALUI HASAN PARVEJ KAUSHIK BERA ANIRBAN PRADHAN NAYIM SEPAY SWARNALI PAUL UMESH CHANDRA HALDER

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      Amyloids, a well-ordered b-sheet-enriched structural network, can be broadly defined as insoluble protein aggregates that are linked to a wide variety of diseases including systemic amyloidosis and some neurodegenerative disorders. Ferulic acid (FA), a phenolic acid, abundant in antioxidant and efficientpharmaceutical has beneficial effects against several ailments. Based on this, we have investigated the protective role of FA on amyloid formation of bovine b-lactoglobulin (b-lg), a model globular protein. Using a set of in vitro biophysical methods, such as UV-Vis spectroscopy, fluorescence, circular dichroism,transmission electron microscopy, etc., our research group has concluded that FA significantly inhibits the heat-induced amyloid formation of b-lg and this inhibitory effect is dose-dependent. Exposed surface hydrophobicity of b-lg amyloid fibrils decreased significantly in the presence of FA. Docking study revealed that ionic and hydrogen bonding interactions between FA and b-lg prevented protein conformational changes leading to fibrillation. We anticipate that our finding would give an insight into the protein aggregation inhibited by the antioxidant compound, FA and pave the way for finding and developing other new small molecules (protein misfolding inhibitors) that give similar result against amyloid fibril formation and its allied neurodegenerative disorders.

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