Browsing by Author "Kundu, Rituparna"
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Item Developing Dirhodium-Complexes for Protein Inhibition and Modification & Copper-Catalyzed Remote Chlorination of Alkyl-Hydroperoxides(2013-09-16) Kundu, Rituparna; Ball, Zachary T.; Marti, Angel A.; Biswal, Sibani LisaThe work describes the development of a new class of protein-inhibitors for protein-protein interactions, based on metallopeptides comprised of a dirhodium metal center. The metal incorporation in the peptide sequence leads to high increase in binding affinity of the inhibitors. The source of this strong affinity is the interaction of histidine on the protein surface with the rhodium center. In addition to this work, rhodium-based small molecule inhibitors for FK-506 binding proteins are investigated. Also, methodology for rhodium-catalyzed modification of proteins containing surface cysteine has been developed where a simple rhodium(II) complex catalyzes cysteine modification with diazo reagents. The reaction is marked by clean cysteine selectivity and mild reaction conditions. The resulting linkage is significantly more stable in human plasma serum, when compared to common maleimide reagents. Apart from this body of work in chemical-biology, the thesis contains the discussion of development of copper-catalyzed remote chlorination of alkyl hydroperoxides. The atom transfer chlorination utilizes simple ammonium chloride salts as the chlorine source and the internal redox process requires no external redox reagents.Item Hybrid organic-inorganic inhibitors of a PDZ-peptide interaction that regulates CFTR endocytic fate(Wiley-VCH Verlag, 2012) Kundu, Rituparna; Cushing, Patrick R.; Popp, Brian V.; Zhao, Yu; Madden, Dean R.; Ball, Zachary T.Item Small molecule conjugates with dimetal species for protein inhibition(2015-06-02) Ball, Zachary T.; Kundu, Rituparna; Popp, Brian V.; Madden, Dean R.; Cushing, Patrick R.; Rice University; Trustees of Dartmouth College; United States Patent and Trademark OfficeMethods for targeting a protein by providing an inhibitor covalently linked to a rhodium(II) complex, introducing the inhibitor to the target protein and allowing the inhibitor and protein to interact. The rhodium(II) complex covalently linked to the inhibitor binds the target protein both inorganically and organically and forms stabilizing secondary contacts between the rhodium(II) complex and the protein.