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MediChem Enters Two-year Deal to Determine Protein Structures for Neurocrine Biosciences

NEW YORK, June 26 - MediChem Life Sciences has agreed to a two-year deal to crystallize and determine three-dimensional protein structures for Neurocrine Biosciences, the companies said Tuesday.

Neurocrine will provide MediChem with clones for a specific G-protein coupled receptor called CRF-1, or corticotropin releasing factor receptor 1, and MediChem--through its subsidiary Emerald Biostructures--will attempt to crystallize the protein alone and with certain ligands that Neurocrine will provide. To determine the 3-D structures of the proteins and the protein-ligand complexes, MediChem will perform x-ray crystallography using the synchrotron facility at Argonne National Laboratory in Argonne, Ill.

In return, Neurocrine, based in San Diego, will pay Chicago-based MediChem to access MediChem's technology, and will provide milestone payments and fees for research services. MediChem also has rights to certain technology that the companies develop from the collaboration.

The deal to provide protein structure determination is the first for MediChem, said Lance Stewart, the president of Emerald Biostructures. But the company would like to sign additional deals. While the company does have its own internal drug discovery and protein characterization efforts, it envisions itself as a provider of drug discovery services and hopes to partner with big pharma to shepherd a potential therapeutic into clinical trials, Stewart said.

From preliminary studies, Neurocrine believes the CRF-1 receptors have potential as therapeutics for depression, anxiety, and irritable bowel syndrome. But the proteins are notoriously difficult to crystallize because they reside in cell membranes. Because these particular proteins are highly regulated, they are difficult to overexpress, Stewart said, and their hydrophobicity makes crystallizing the protein a significant challenge.

However, Stewart said MediChem has acquired expertise in tackling these issues, by hiring Craig Behnke, who helped solve the crystal structure of rhodopsin, and by licensing technology from the University of California, San Francisco, for automatically arranging membrane proteins in lipidic cubic phase. This technology can facilitate protein crystallization. Additionally, MediChem's access to a beamline at the Argonne synchotron, made possible through a preferred user's agreement, provides a powerful source of tunable x-rays.

"To get these kinds of deals it's required to show that you have some expertise," said Stewart. "But keep in mind that no one has proven themselves capable of solving every crystal structure. There's still a lot of demonstration that still needs to go on."
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