Pharmaceutical Sciences and Natural Products - Research Publications

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Author: search.filters.author.Kaur, ManpreetHas files: Yes

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    C‐N and N‐N bond formation via Reductive Cyclization: Progress in Cadogan /Cadogan‐Sundberg Reaction.
    (wiley, 2018) Kaur, Manpreet; Kumar, Raj Kumar
    Cadogan/Cadogan‐Sundberg cyclization reaction has been reported as one of the most efficient routes for the synthesis of a wide variety of N‐heterocycles from the easily accessible starting materials such as o‐nitrobiaryls or o‐nitroarenes, o‐nitrostyrenes by treating with tetravalent phosphorus compounds (trialkyl or triaryl phosphines or trialkyl phosphites). The reaction has been successfully employed in Carbon‐Carbon as well as Carbon‐Nitrogen bond formation for the scaffolds like carbazole, indoles, coumarins, and indazoles. To the best of authors’ knowledge, the present review is the first compilation of the literature from almost two decades (2000 to present) on Cadogan/Cadogan‐Sundberg cyclization reaction, its scope, mechanistic aspects, and limitations.
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    Toward an Understanding of Structural Insights of Xanthine and Aldehyde Oxidases: An Overview of their Inhibitors and Role in Various Diseases
    (John Wiley and Sons Inc., 2018) Kumar, Raj; Joshi, Gaurav; Kler, Harveen; Kalra, Sourav; Kaur, Manpreet; Arya, Ramandeep
    Almost all drug molecules become the substrates for oxidoreductase enzymes, get metabolized into more hydrophilic products and eliminated from the body. These metabolites sometime may be more potent, active, inactive, or toxic in nature compared to parent molecule. Xanthine oxidoreductase and aldehyde oxidase belong to molybdenum containing family and are well characterized for their structures and functions, in particular to their ability to oxidize/hydroxylate the xenobiotics. Their upregulated clinical levels causing oxidative stress are associated with pathways either directly involved in the progression of diseases, gout, or indirectly with the succession of other diseases such as diabetes, cancer, etc. Herein, we have put forth a comprehensive review on the xanthine and aldehyde oxidases pertaining to their structures, functions, pathophysiological role, and a comparative analysis of structural insights of xanthine and aldehyde oxidases? binding domains with endogenous ligands or inhibitors. Though both the enzymes are molybdenum containing and are likely to share some common pathways and interact with inhibitors in a similar manner but we have focused on structural prerequisites for inhibitor specificity to both the enzymes keeping in view of the existing X-ray structures. This review also provides futuristic implications in the design of inhibitors derived from inorganic complexes or small organic molecules considering the spatial features and structural insights of both the enzymes. ? 2017 Wiley Periodicals, Inc.