Abstract
a Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Kafrelsheikh University, Kafrelsheikh, Egypt. b Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Tanta University, El Giesh street, 31527, Tanta, Egypt. c Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Tanta University, El Giesh street, 31527, Tanta, Egypt. d Department of Pharmacology and toxicology, Faculty of Pharmacy, Tanta University, El Giesh street, 31527, Tanta, Egypt.
Highlights
Cancer is one of the leading causes of death in the world, in developing countries (WHO Fact sheet on cancer, 2015)
Molecular docking study was performed to interpret the comparative differences in the binding interactions of the synthesized novel compounds at molecular level as inhibitors of human dihydrofolate reductaseand to understand the structure activity relationships
Dihydrofolate reductase (DHFR) inhibition has long been identified as an important target for the development of chemotherapeutic agents against bacterial and parasitic infections as well as cancer(Anderson and Wright, 2014; Al-Rashood et al, 2014).This considerable pharmacological interest in dihydrofolate reductase (DHFR) is due to that enzyme inhibition results in depletion of intracellular reduced folates necessary for one-carbon transfer reactions which, in turn, are important for the biosynthesis of thymidylate
Summary
Cancer is one of the leading causes of death in the world, in developing countries (WHO Fact sheet on cancer, 2015). Several studies based on the triazine scaffold toward antitumor activity have been carried out (Ma and Chui, 2010) starting by Baker who studied active site-directed inhibition of hDHFR enzyme (Baker and Lourens, 1967). These compounds are inhibitors of DHFR and are clinically promising for use in cancer chemotherapy (Camerman et al, 1978)
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