Chicago, IL - August 27, 2001 - Corvas International, Inc. (Nasdaq: CVAS) reported today that Company scientists and collaborators at the Max-Planck Institute of Biochemistry in Martinsried, Germany, have solved the three-dimensional molecular structure of the functional domain of matriptase, a newly identified serine protease target for breast and prostate cancer drug development. This new structural information is expected to facilitate the design of drugs that block or otherwise exploit the activity of matriptase and related proteases. Corvas also presented its strategy for the discovery and development of new solid tumor cancer therapies that target the serine protease gene family at the 222nd National Meeting of the American Chemical Society today in Chicago, IL.
Matriptase is the first member of a distinct family of cancer-associated, transmembrane serine proteases to be characterized at the molecular level, said Edwin Madison, Ph.D., Vice President of Biological Research, who presented for Corvas. We intend to use matriptase as a target itself and as the model protease for this gene family to accelerate the rational design and optimization of drugs to treat solid tumor cancers. With our collaborators at Max-Planck, we have already generated several proprietary high resolution 3-D structures of matriptase bound to lead small molecule inhibitors. Inhibitors have therapeutic potential as drugs for the treatment or prevention of disease and are used as research tools to validate the role of proteases in disease.
Unlike most proteases, which are either secreted from or retained in the cell, transmembrane serine proteases are located on the cell surface of tumor cells. This confined location may offer a unique opportunity to target cancer treatments directly to diseased tumor cells th
Contact: Virginia Amann
Atikins + Associates