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Abstract

HOMOLOGY MODELING AND E-PHARMACOPHORE MAPPING OF DIHYDROPTEROATE SYNTHASE 1 ENZYME OF MYCOBACTERIUM LEPRAE

Mahesh Kumar*, Jagbir Singh, Akash Deep, Rani Mansuri

ABSTRACT

Worldwide, about 250,000 new cases of leprosy are reported each year and about two million people have leprosy related disabilities. Due to main drugs resistance and multidrug resistance there is need of crucial drug target identification and potential drugs. Dihydropteroate synthase 1 enzyme coded by the gene folP1 found to have nill similarity with human genome. Dihydropteroate synthase 1 enzyme is found to be responsible for the formation of the immediate precursor of folic acid used in biosynthesis of tetrahydrofolic acid (tetrahydrofolate, THF), the active form of folic acid (vitamin B9). Folic acid is an essential vitamin (B9), which plays a key role in the methylation cycle and in DNA biosynthesis. So inhibition of particular enzyme can lead to death of mycobacterium leprae. In present research effort homology model will be made and e-pharmacophore mapping will be done on the basis of interaction analysis of target model with pterin monophosphate an endogenous ligand. 3D model of target protein (Dihydropteroate synthase 1) can used for structure based drug designing. Potent inhibitors for target protein model can be designed on the basis of e-pharmacophore hypothetical model.

Keywords: MDR, Folic acid, Dihydropteroate synthase 1, pterin monophosphate, epharmacophore, MacroModel.


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