Parniak has spent more than 15 years studying the RNase H enzyme and developing antiviral drugs for HIV/AIDS, and he and Sarafianos have collaborated on research projects for more than six years. Together, they solved the framework of an RNase H fragment, mapping out the molecular details of its crystal structure and providing a roadmap for their current research.
"If we know what the lock looks like, we can make the key," Sarafianos said. "Knowing the crystal structure gives us the framework for designing the most potent compounds that target the RNase H enzyme, which is a novel and key target for antiretroviral drug discovery."
Parniak, an expert in virology and pharmacological analysis, has identified more than 3,000 different leads for compounds that could target RNase H. However, he said it's Sarafianos' expertise and experience in crystal structures that will allow them to design the best compounds that will be then synthesized at the University of Minnesota.
"Dr. Sarafianos brings a fresh approach," Parniak said. "He has the perfect combination of skills and knowledge to move this project forward. If anyone can solve this, it's him."
In addition to targeting the HIV virus, the behavior present in the RNase H enzyme is also present in more common viruses, such as Hepatitis B. Two billion people worldwide have been infected with the Hepatitis B virus, and about 600,000 people die every year as a result of Hepatitis B infection.
"The knowledge that we gain for developing drugs against the RNase of HIV could eventually be applied toward designing dr
|Contact: Laura Gerding|
University of Missouri School of Medicine