Publications by authors named "Sayani Sarkar"

Starch-based biofilms are biodegradable, but their application is limited by lower mechanical strength and absence of antimicrobial properties. In this context, the present study attempted to unleash the potential of nanotechnology for synthesizing nano-starch (NS) and tannic acid-coated nano-starch (T-NS) for augmenting the tensile strength and antimicrobial properties of starch-based biofilms. Moreover, this study reports one of the first such attempts to improve the commercial viability of starch extracted from the corms of Amorphophallus paeoniifolius.

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is one of the causing agents of nosocomial infections. A wide range of antibiotics fails to work against these pathogens. Hence, there is an urgent requirement to develop other therapeutics to solve this problem.

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Ubiquitin RING E3 ligases (E3s) catalyze ubiquitin (Ub) transfer to their substrates by engaging E2∼Ub intermediates with the help of their RING domains. Different E3s have been found to contain a conserved tryptophan residue in their RING that plays an essential role in E2 binding and, hence, enzymatic activity. Many active E3s, however, lack this specific residue.

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Development of a gastroretentive sustained release tablet of metformin based on poly (acrylic acid)-grafted-gellan (PAAc-g-GG) is the main purpose of this study. At first, PAAc-g-GG was synthesized by microwave-promoted free radical initiation method using cerric (IV) ammonium nitrate (CAN) as redox initiator and characterized by elemental analysis, FTIR, DSC-TGA, C NMR, biodegradation and viscosity study. The synthetic parameters were optimized by 2 full factorial design using Design Expert software.

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Ubiquitination of a target protein is accomplished through sequential actions of the E1, E2s, and the E3s. E2s dictate the modification topology while E3 ligases confer substrate specificity and recruit the cognate E2. Human genome codes for ~35 different E2 proteins; all of which contain the characteristic ubiquitin-conjugating UBC core domain sufficient for catalysis.

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