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The existing screening systems for anti-hepatitis B virus (anti-HBV) drug discovery is time-consuming mainly due to the laborious detection system it is using. A new fluorescence based screening system for high throughput anti-HBV drug discovery was created by tagging hepatitis B surface antigen (HBsAg) with monomeric red fluorescent protein and hepatitis B virus (HBV) core protein with enhanced green fluorescent protein. The two constructs were co-transfected on to Hep3B cells and the transfection was stabilized by fluorescent activated cell sorter (FACS). The fusion proteins expressed through the secretory protein pathway as evidenced by localization with ER-Tracker and tubulin tracker. The new system has given analogues results like that of conventional enzyme-linked immunosorbent assay (ELISA). Hence it can be of very high potential for large scale drug screening systems. [ABSTRACT FROM AUTHOR]

• The electrochemical synthesis of precursor to biologically active C-nucleosides was carried out. • An enzyme based bioelectrocatalysis for the oxidation of d -ribofuranose to d -ribonolactone, precursor of Remdesivir was developed. • The electrochemical oxidation was carried out on laccase immobilized poly-thiophene supported carbon fiber paper. • The screening of the reaction condition and plausible mechanism of the reaction were established. A modified electrode based on laccase immobilized poly-thiophene-3-carboxylic acid supported on carbon fiber paper was developed for the electrocatalytic oxidation of D-ribofuranose to otherwise difficult-to-access D-ribonolactone, a precursor for C-nucleoside based drug like Remdesivir. The electrochemical oxidation of D-ribofuranose was achieved by the TEMPO-mediated electrochemical process. The experimental parameters were optimized and validated using Design of Experiment (DoE) statistical tool indicating the concentration of TEMPO and stirring as important parameters in bulk electrolysis. The mechanism for the electrochemical oxidation of D-ribofuronose followed single electron anodic oxidation of TEMPO mediated by laccase to the corresponding oxoammonium nitrosonium species which was vital for the mediated electrochemical oxidation. The mechanism for the electrochemical oxidation was established using cyclic voltammetry and computational studies. The plausible interactions of laccase enzyme with TEMPO mediator were studied using molecular docking experiments. This facile method was successfully applied for the oxidation of D-ribofuranose to D-ribonolactone. [Display omitted] [ABSTRACT FROM AUTHOR]