Hepatitis B Foundation

Bucks County's Institute for Hepatitis and Virus Research and BioLeap Collaborate on New Discoveries

Collaboration Unveils Novel Compounds for the Treatment of Hepatitis C


New Hope, PA -- (ReleaseWire) -- 10/10/2007 -- Bucks County’s Institute for Hepatitis and Virus Research (IHVR) and BioLeap have entered into a collaboration to develop new therapeutic compounds for the treatment of Hepatitis C. Up to 50% of patients treated with current standard therapies do not respond adequately and often suffer serious side effects from the drugs. Thus there is a critical need for new tools to treat this disease. By combining BioLeap’s leading edge computational fragment-based design capabilities with the IHVR’s extensive experience and in-depth knowledge of viral diseases, the collaboration will result in new classes of lead drug molecules with novel modes-of-action.

Of particular interest to the IHVR is BioLeap’s proprietary technology that rapidly calculates the free energies, or affinities of interactions between small molecular fragments of potential drugs and biomolecular structures of the proteins they will target, displaying the distribution and orientation of these fragments. This information provides a unique insight into how small molecules bind into key protein binding sites that cannot be achieved from the static crystal structure alone, or from methods that can only measure the enthalpic properties of binding. In addition to lead discovery, the quantitative free-energy based analysis of protein-drug-fragment interactions adds significant value to the lead optimization process. In combination, this proprietary approach provides chemists and biologists the information they need to assemble, fragment by fragment, a completely new molecule that not only optimally binds to the targeted protein site but also has properties desirable in a drug, including solubility and bioavailability.

Commenting on the collaboration, BioLeap’s Gerry Evans, Executive Vice President of BioLeap, noted: “Dr. Tim Block and his team at the IHVR are renowned for their work in this field. We are very excited by the opportunity to focus our combined expertise on this important target.”

Dr. Tim Block, president of the IHVR, is enthusiastic about the prospects for this collaboration. “One approach in discovering new treatments is the time and labor intensive process of screening tens or hundreds of thousands of molecules from compound libraries. BioLeap’s technology provides a potential shortcut by eliminating the need to screen compound libraries, while significantly broadening the field of chemical diversity. The molecules designed by BioLeap are not limited by what is present in any compound library. This greatly increases our odds of finding a potential drug that precisely targets the hepatitis C virus and that will not easily succumb to viral resistance. Once BioLeap has identified several candidate molecules, our scientists will test their effectiveness on the hepatitis C virus. Based on these results, we will repeat this iterative process until we have found the ideal drug.”

About the Institute for Hepatitis and Virus Research:
Established as the research arm of the Hepatitis B Foundation, the mission of the Institute for Hepatitis and Virus Research is to use discovery science to find new therapies for viral hepatitis and liver cancer; to advance its research discoveries through traditional scholarship and educational opportunities; to nurture biotechnology through technology transfer and new company formation; and to promote public health outreach programs to improve the quality of life for those with viral hepatitis.

About BioLeap:
Bioleap is a leader in computational fragment-based drug design. The company’s proprietary design technology and process successfully addresses one of the biggest problems in preclinical drug discovery: limited chemical diversity of compound libraries. Development collaborations span a broad spectrum of target proteins including: kinases, nuclear hormone receptors, metalloenzymes, and metalloproteases.