CAMBRIDGE, U.K., March 25, 2002 (PRIMEZONE) -- Astex Technology, the structure-based drug discovery company, announced today that it has received the first milestone payment from AstraZeneca AB, as part of a structural biology research agreement focused on solving novel human cytochrome P450 crystal structures. The payment is related to Astex' determination of the first 3-dimensional structure of a human cyotchrome P450 enzyme, announced at the end of 2001.
Timothy Haines, Chief Executive of Astex, said, "The progress Astex has made in the determination of human P450 crystal structures and the attainment of this significant milestone has been recognized by AstraZeneca, endorsing the company's abilities in structure-based drug discovery. Determination of the structures of additional human P450s is underway, and will continue to provide invaluable information for the rational design of drugs with reduced metabolic and toxicity problems."
Astex Technology is a structure-based drug discovery company pioneering the use of high throughput X-ray crystallography for the rapid identification of novel drug candidates. The company's unique structural screening approach utilizes protein crystal structures to detect the binding of drug fragments, which are then optimized into potent lead compounds. Facilitating this approach is the company's integrated drug discovery platform of HTX(R) technologies, which covers all aspects of structure-based research, including protein production, crystallization, structure determination, bioinformatics and computational and medicinal chemistry. Astex is focusing its drug discovery approaches on proprietary and public domain protein targets from families and/or pathways. This includes validated kinases, phosphatases and proteases implicated in human disease. Astex has research agreements with Johnson & Johnson Pharmaceutical Research and Development focused on lead discovery and optimization, and structural biology research agreements with AstraZeneca AB and Aventis Pharmaceuticals focused on solving novel cytochrome P450 crystal structures.