Antiviral Azide Containing Compounds

Unmet Need: Viral infections in humans, animals, plants and insects lead to many societal burdens including disease and agricultural loss. Most anti-viral treatment strategies to date are limited in scope to the virus of interest and often result in drug resistance, incomplete efficacy, and/or toxicity. Costs for viral specific targets can be massive and take years to develop. Therefore, there is an urgent need for broad, effective and safe anti-viral treatments that can attenuate virus infectivity or pathogenesis.

Technical Details: Researchers have developed a novel strategy for expansively treating viral infections through inhibition of infectivity using azide-modified biomolecules. Biomolecules include fatty acids, carbohydrates and lipids that are involved in post-translational modifications for many viruses, allowing for the technology’s broad use. As shown in vitro, azide-modified lipids incorporated post-translationally on proteins of human HIV-1 or insect baculovirus led to decreased infectivity of both viruses compared to unlabeled controls. Azide-modified fatty acids can be added simply as a dietary source and are orally bioavailable requiring no specialized delivery. In addition, modified biomolecules can be used to label viral proteins in vivo to monitor viral infectivity. Finally, altering modification from an azide to alkyne group has shown the opposite effect of increasing infectivity as a strategy to aid propagation of viral stocks for vaccine development or vector delivery.

Value Proposition:

·      Novel anti-viral treatment strategy targeting common viral process of post-translational modification

·      Azide-modified biomolecules decrease infectivity in broad range of viruses

·      Treatment can be administered alongside currently accepted antiviral drugs for increased efficacy

Looking for Partners to: Develop & commercialize the technology as a novel anti-viral treatment strategy.

Stage of Development: Pre-Clinical

Data Availability: In vitro 

Publication(s): Colquhoun DR, Lyashkov AE, Mohien CU, Aquino VN, Bullock BT, Dinglasan RR, Agnew BJ, Graham DRM. (2015) Bioorthogonal mimetics of palmitoyl-CoA and myristoyl-CoA and their subsequent isolation by click chemistry and characterization by mass spectrometry reveal novel acylated host-proteins modified by HIV-1 infection. Proteomics 15(12):2066-77.