FDA approves Lab's cancer treatment technology
The U.S. Food and Drug Administration has approved a Lawrence Livermore-developed cancer treatment tool. Peregrine, named after the patron saint of cancer patients, is a computer-based system for calculating where radiation goes in the body. It allows doctors to more accurately target tumors with radiation, permitting them to increase the dose needed to eradicate tumors without increasing damage to healthy surrounding tissues.
Peregrine has been under development since 1994 by the Laboratory, in collaboration with researchers at the University of California at San Francisco and other academic institutions. Along the way, it has won the prestigious R&D 100 Award and a Federal Laboratory Consortium technology transfer award. Its principal investigator, Christine Hartmann Siantar, was named a Teller Fellow for her work on the project.
Peregrine combines the Laboratory's 50 years of expertise in radiation physics with advanced computer architectures to produce a system that determines radiation dose information in minutes. Using the Monte Carlo mathematical technique, it simulates the trillions of radiation particles that enter the body during treatment and accurately predicts the energy-that is, the radiation dose-deposited by the particles. The system uses a patient's computed tomography scans to tailor precise radiation doses based on that individual's anatomy and disease.
The Laboratory is partnering with NOMOS Corporation of Pennsylvania, a leading supplier of radiation treatment technologies, to bring Peregrine systems to the medical community. NOMOS will deploy Peregrine on its CORVUS radiation treatment system to accurately calculate the actual dosage for each patient.
Peregrine resulted from a multidisciplinary research effort at the Laboratory. Its development required the expertise of physicists, computer scientists, and electrical engineers, among others. Rosemary Walling, the current program manager of Peregrine, says of the FDA approval, "This was not just about physics. Everyone worked hard to see this project get the validation and verification it needed to get it through to a commercial channel." Now, says Hartmann Siantar, "Peregrine will touch lives. It is a breakthrough technology that could be used in treatment clinics everywhere."
Contact: Christine Hartmann Siantar (925) 422-4619 (firstname.lastname@example.org).
Growing protein crystals to fight tuberculosis
The Macromolecular Crystallography and Structural Genomics group at the Laboratory will receive a $4-million grant to perform research to aid the design of tuberculosis drugs. The work will be a key component of a National Institutes of Health-funded program to fight tuberculosis, the number-one infectious disease in the world. The NIH program involves 6 nations and 13 institutions. It will be led by Los Alamos National Laboratory, which is receiving a 5-year, $28-million grant to coordinate the work and distribute the funds.
The Livermore team, led by Bernhard Rupp, will provide crystals of more than 400 proteins of the tuberculosis bacterium. Specific proteins are the means by which the tuberculosis bacterium invades cells and unleashes its virulence; therefore, the proteins are the prime targets for drug intervention. The molecular structure of those proteins must be known in detail so scientists can design effective, specific drugs to interact with them, and crystals are the means of determining the structures.
The Macromolecular Crystallography team will design computer-controlled, robotic devices that enable fast production of protein crystals. Rupp says that it will take "many, many experiments to find the proper conditions in which this crystal forms." After the crystals are made, the researchers will expose them to x radiation. The patterns of x-ray diffraction can then be used to reconstruct three-dimensional protein molecular structures.
"Obtaining crystals of proteins is a key challenge in determining the molecular structure," says Rupp. "Without crystals, there is no crystallography. Proteins are complex biological material, and protein crystals thus are fragile and difficult to grow." Rupp says the team has had great success in crystallizing a variety of bacterial pathogens and determining the structures of tetanus and botulinum toxins. "We are excited about the possibilities of making significant contributions to the understanding and the final defeat of TB. Drug design is at the forefront of biomedical research and a great challenge for the whole TB structural genomics team."
The tuberculosis research program is one of seven NIH pilot studies that build on the discoveries of the government's Human Genome Project and other DNA sequencing research.
Contact: Bernhard Rupp (925) 423-3273 (email@example.com).
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