From Two Technologies, Many Applications
Detector proteins change color to signal the presence of a hazardous pathogen or other substance. They detect enzymes secreted only by the specific pathogenic bacteria of interest. They don't react to dead bacteria, nor will they trigger a false alarm in the presence of harmless bacteria, foodstuffs or mammalian tissue.
"If you do a lot of genome-gazing, you appreciate the fact that there are a lot of common mechanisms by which these bacteria infect and cause inflammation, which leads to everything from local irritation to wound infection to meningitis," says Mitch Sanders, head of Worcester-based ECI Biotech.
According to ECI literature, detector proteins work quickly, are selective and inexpensive to produce, and can be incorporated into a wide array of potential products. Here are some examples:
Food Safety and the Environment
- A swab test for meat processing plants that would glow fluorescent green if a food pathogen such as Listeria monocytogenes is present
- A sensor for plastic bags containing leftovers that would change color if food is spoiled
Lead and Heavy Metals
- A rapid-read lead-level diagnostic test that uses saliva (current tests, done mostly on children, require a blood sample)
- A disposable wipe that removes and encapsulates toxic lead dust from walls and other surfaces
- A badge that would alert the wearer to a broad spectrum of bacterial and viral agents, including anthrax, smallpox and plagues
- Proteins that would bind to toxic heavy metals, removing them from public water supplies, or to uranium and other radioactive residue from "dirty bombs"
Protector proteins act by stabilizing the structure of important cell proteins. To function, protein chains must remain folded in a specific three-dimensional shape, but environmental and chemical stresses, such as heat or pH changes, can turn them into useless tangles.
Under the right conditions, protector proteins can coax partially unfolded protein chains back into their proper shape. If employed in the early phase of healing, they can protect the assaulted protein chains and increase their production of needed enzymes.
"We think these proteins will alleviate a lot of the inflammation and irritation to allow the healing process to occur," Sanders says. "Put this stuff in a gel, slap it on a wound, and you'll make the cells more viable so they'll recover faster. We've shown that we can actually prevent cells from dying when they're cooked in an oven."
ECI is currently pursuing off-site studies with pigskin, which is remarkably similar to human skin. "It's a little pie-in-the-sky," cautions Sanders, "but if it works, it could be a tremendous opportunity."
One important application that Sanders is considering would incorporate protector proteins and detector proteins to produce advanced wound-care products. He envisions a bioactive wound dressing made of a plastic-coated spongy material.
Detector proteins in the dressing would allow caregivers to tell at a glance if an infection is developing, before an immune reaction or sepsis (blood-borne infection) occurs. Immediate treatment would result in faster recovery, fewer complications and lower health care costs. Meanwhile, protector proteins would promote cell growth and healing at the molecular level. --JKMtransformations@wpi.edu
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Last modified: Sep 02, 2004, 11:07 EDT