1404217-67-9Relevant academic research and scientific papers
Acyclic phosph(on)ate inhibitors of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase
Clinch, Keith,Crump, Douglas R.,Evans, Gary B.,Hazleton, Keith Z.,Mason, Jennifer M.,Schramm, Vern L.,Tyler, Peter C.
, p. 5629 - 5646 (2013/09/02)
The pathogenic protozoa responsible for malaria lack enzymes for the de novo synthesis of purines and rely on purine salvage from the host. In Plasmodium falciparum (Pf), hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT) converts hypoxanthine to inosine monophosphate and is essential for purine salvage making the enzyme an anti-malarial drug target. We have synthesized a number of simple acyclic aza-C-nucleosides and shown that some are potent inhibitors of Pf HGXPRT while showing excellent selectivity for the Pf versus the human enzyme.
