Please use this identifier to cite or link to this item: http://hdl.handle.net/10266/5849
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dc.contributor.supervisorChhibber, Manmohan-
dc.contributor.supervisorSaxena, Sanjai-
dc.contributor.authorKaur, Arashdeep-
dc.date.accessioned2019-10-04T06:03:59Z-
dc.date.available2019-10-04T06:03:59Z-
dc.date.issued2019-10-04-
dc.identifier.urihttp://hdl.handle.net/10266/5849-
dc.descriptionM.Sc Thesis of Arashdeep Kauren_US
dc.description.abstractGout is a medical condition characterized by increase of the serum urate levels (sUAs) in extra- cellular fluids that results in its precipitation in the tissues causing joint swelling, uric acid stones and further complications if not cured. Xanthine oxidase (XO) and xanthine oxidoreductase (XOR) are two inter convertible enzymes responsible for uric acid production from hypoxanthine and xanthine. It has been reported that increased expression of XO leads to excessive oxidative stress leading to the formation of ROS and ultimately uric acid. Therefore, inhibitors of XO can act as a drug to treat conditions leading to hyperuricaemia and gout. Allopurinol and febuxostat are two molecules presently in use for the treatment of this medical condition that work by inhibition of XO. Present work involved selection of known XO inhibitors from literature and exploration of their mechanism for inhibition using in-silico docking studies. After an extensive literature search nine compounds belonging to flavanone and cinnamic acid derivatives were shortlisted along with Pinobanksin (flavones), ursolic acid and umbelliferone. All the compounds were docked against “de-molybednum rat xanthine oxidoreductase D428A enzyme” that showed pinobanksin as the best inhibitor due to its flexible nature at C-3 carbon having sp3 hybridization. However, studies on human XO and XOR enzyme need to be done both in-silico and in wet experiments for development of these molecules as active drugs.en_US
dc.language.isoenen_US
dc.subjectGouten_US
dc.subjectUric Aciden_US
dc.subjectXanthine oxidaseen_US
dc.subjectXanthine oxidoreductaseen_US
dc.subjectInhibitors of XOen_US
dc.subjectDocking Studiesen_US
dc.subjectIC50en_US
dc.titleDocking Studies of De Molybednum Rat Xanthineoxidoreductase D428A Mutant Enzyme with Polyphenolsen_US
dc.typeThesisen_US
Appears in Collections:Masters Theses@SCBC

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