Publications by authors named "Sneha Wankar"

Considering the rapidly increasing population, the development of new resources, skills, and devices that can provide safe potable water and clean energy remains one of the vital research topics for the scientific community. Owing to this, scientific community discovered such material for tackle this issue of environment benign, the new materials with graphene functionalized derivatives show significant advantages for application in multifunctional catalysis and energy storage systems. Herein, we highlight the recent methods reported for the preparation of graphene-based materials by focusing on the following aspects: (i) transformation of graphite/graphite oxide into graphene/graphene oxide exfoliation and reduction; (ii) bioinspired fabrication or modification of graphene with various metal oxides and its applications in photocatalysis and storage systems.

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The present work envisioned to synthesize europium complexes [Eu-(L)-phen] (where, L is 4,4,4-Trifluoro-1-(2-furyl)-1,3-butanedione (TFB), phen-1,10 -phenanthroline) and its hybrids via embedding pure complex into silica and PMMA. The sol-gel method was adopted for incorporating europium complex into silica matrix as [Eu-(L)-phen]-silica and this method was proved to be highly effective and excellent approach for obtaining such lanthanide hybrid material. Another hybrid was prepared by incorporating complex into PMMA (polymethyl methyl acrylate), an organic polymer, transformed into flexible thin film.

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The principal intent of this work is to explore whether the site-specific binding of a newly synthesized quinoline-appended anthracenyl chalcone, ()-3-(anthracen-10-yl)-1-(6,8-dibromo-2-methylquinolin-3-yl)prop-2-en-1-one (ADMQ), with an extracellular protein of the human circulatory system, human serum albumin (HSA), can control the rotamerization of its sole tryptophan residue, Trp-214. With this aim, we have systematically studied the binding affinity, interactions, and localization pattern of the title compound inside the specific binding domain of the transport protein and any conformation alteration caused therein. Multiple spectroscopic experiments substantiated by an in silico molecular modeling exercise provide evidence for the binding of the guest ADMQ in the hydrophobic domain of HSA, which is primarily constituted by residues Trp-214, Arg-218, Arg-222, Asp-451, and Tyr-452.

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Lanthanide complexes of p-nitrobenzoic acid(p-NBA) and o-phenanthroline(o-phen) namely [Ln2(Phen)2(p-NBA)3(NO3)2].2H2O where, Ln = Sm(III),Tb(III),Dy(III) and [Eu2(Phen)2(p-NBA)3].4H2O were synthesized and further characterized by Elemental analysis, UV spectroscopy, IR spectroscopy, (1)HNMR spectroscopy.

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