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Dnyaneshwar S. Raut

Researcher at University of Calabria

Publications -  11
Citations -  271

Dnyaneshwar S. Raut is an academic researcher from University of Calabria. The author has contributed to research in topics: Catalysis & Ionic liquid. The author has an hindex of 7, co-authored 11 publications receiving 231 citations. Previous affiliations of Dnyaneshwar S. Raut include National Chemical Laboratory.

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Ionic liquid promoted synthesis, antibacterial and in vitro antiproliferative activity of novel α-aminophosphonate derivatives.

TL;DR: Compounds 4b, 4c, 4d, 4f and 4j were found more potent antibacterials against pathogenic microorganisms and compound 4j was found a promising antiproliferative agent against A549 and SK-MEL2 human melanoma cell lines.
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Diversity-oriented synthesis of α-aminophosphonates: a new class of potential anticancer agents.

TL;DR: Surprisingly, compound 4n having (R)-1-phenylethanamine was found to be the most active amongst all the synthesized α-aminophosphonates against all the five cancer cell lines, most prominent being against Jurkat cell line with an IC50 value of 4 μM.
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Catalytic Oxidative Carbonylation of Amino Moieties to Ureas, Oxamides, 2-Oxazolidinones, and Benzoxazolones.

TL;DR: It is found that it is possible to perform the direct syntheses of ureas, oxamides, 2-oxazolidinones, and benzoxazolones by the oxidative carbonylation of amines, β-amino alcohols, and 2-aminophenols using the PdI2 /KI catalytic system in an ionic liquid.
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A Palladium-Catalyzed Carbonylation Approach to Eight-Membered Lactam Derivatives with Antitumor Activity.

TL;DR: In this article, the reactivity of 2-(2-alkynylphenoxy)anilines under PdI2 /KI-catalyzed oxidative carbonylation conditions has been studied.
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An efficient synthesis of benzodiazepinyl phosphonates as clostripain inhibitorsviaFeCl3 catalyzed four-component reaction

TL;DR: The synthesized BDPs have shown significant protease inhibition activity against clostripain, a disease model for gas gangrene, suggesting that these novel chemical entities could be further explored as cysteine protease inhibitors.