Washington Editor
The National Institutes of Health awarded Structural GenomiX Inc. the authority to manage $18.1 million over three years in a public-private venture focused on protein structure research.
Structural GenomiX (SGX) will share the funding with other New York Structural Genomics Research Consortium participants, including scientists at the Albert Einstein College of Medicine, the Brookhaven National Laboratory, Columbia University, The Rockefeller University and the Weill Medical College of Cornell University.
However, SGX, a four-year-old San Diego-based company, is charged with divvying up the money under the direction of Stephen Burley, SGX's chief scientific officer and senior vice president. Burley left his post at Rockefeller earlier this year to accept the job at SGX.
"When he joined SGX, Dr. Burley recognized that the goals of the consortium could be better served by a collaboration between academia and SGX because we have the powerful, automated, high-throughput structural determination platform - the technology that is required to move things faster and better," Karen Silva, SGX's director of corporate communications and investor relations, told BioWorld Today. "Consequently he proposed a scenario to the National Institute of General Medical Sciences [NIGMS of the NIH] and they took it into consideration and it was recently announced that the grant would be transferred to GSX."
She added, "We are particularly gratified that the NIH has recognized the validity and the importance of protein research and the structural determination of proteins, and that a public-private consortium can move the project forward. Now there's no doubt that this particular work is being done in academic labs. However, the NIH has recognized that the technology that has advanced in the private sector can move these projects faster."
The NIGMS Protein Structure Initiative has been in operation for two years and the effort consists of two phases. In the initial pilot phase, teams of scientists across the country are hammering out workable techniques to streamline and automate the multistep process of obtaining protein structure data. The subsequent full-scale production phase will be devoted to researchers deriving the structures as rapidly as possible, leading to a remarkable 10,000 structures in 10 years, according to a statement from SGX.
In the first year, SGX will retain approximately 30 percent of the grant funding, with the remaining 70 percent slated for distribution among the participating not-for-profit research institution collaborators.
Aside from lending Burley's expertise to the project, SGX will be responsible for gene cloning and expression, purification and biophysical characterization of target proteins. SGX will use its proprietary technology platform to produce proteins for crystallization and determination.
Silva said SGX's technology platform "moves the protein crystallization process faster and more efficiently. So, in other words, whereas five years ago it would have taken X number of hours to complete one path, we are able to do it today in a very high, rapid speed."
SGX also will provide the project with access to its state-of-the-art X-ray beamline at the Advanced Photon Source, Argonne National Laboratory, for structure determination efforts.
SGX was founded in 1998 by Barry Honig and Wayne Hendrickson, both professors of biochemistry and molecular biophysics at Columbia University in New York, and Linda Grais, a physician and attorney.
The company has several other ongoing deals, including an agreement signed earlier this year with Anadys, of San Diego, focused on developing antibacterial drugs. Also, the company is involved in a $13 million deal with the Cystic Fibrosis Foundation to decipher the 3-dimensional structure of a protein that, when defective, can cause cystic fibrosis, and it has entered drug discovery deals with Millennium Pharmaceuticals Inc., of Cambridge, Mass., and Aventis Pharmaceuticals Inc., of Bridgewater, N.J. (See BioWorld Today, July 26, 2002; Feb. 9, 2001; and Jan. 8, 2002.)