NOVEL COMPOUNDS FOR TREATMENT OF PARASITIC PROTOZOA

All parasitic protozoans lack the ability to synthesize purine nucleotides. Instead they obtain purine nucleotides solely by salvaging purine bases and/or nuclosides from their host. Purine salvage enzymes like phosphoribosyltransferases (PRTs) play a pivotal role in protozoan purine salvage pathways and are important for their survival. Inhibiting protozoan PRTs could thus represent an efficient approach for treatment of parasitic infections.

Through graphic modeling of the enzyme active site and rational design, researchers at UCSF have developed novel heterocyclic inhibitors of the protozoan PRTs. In vitro, low micromolar concentrations of these compounds effectively inhibit the growth of Tritrichomonas foetus, a parasite that causes bovine trichomoniasis, and Giardia lamblia, a water-borne infectious agent that causes severe diarrhea in humans. These inhibitors have no effect on human PRTs at concentrations up to 1 mM.

Intellectual Property:

UCSF holds two issued U.S. patents (Nos. 6,075,044 and 6,221,877) claiming compositions that inhibit T. foetus and G. lamblia. Both of these patents are available for licensing. Foreign rights are not available.

Select Reference:

Aronov AM et al., Rational design of selective submicromolar inhibitors of Tritrichomonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase. Biochemistry, 2000; 39: 4684-4691.

If you would like to receive further information about this technology and potential licensing opportunities, please contact:

Joel B. Kirschbaum, Ph.D.
Director & Senior Technology Portfolio Manager
(415) 353-4462 phone
(415) 348-1579 fax
Joel Kirschbaum, Ph.D.

Reference: OTM Case #SF97-145, #SF00-067