Scientists determine drug target for the most potent botulinum ...(ernal fluid of the cell. The toxin then ...)

To block the toxins action, the researchers designed four decoy protein fragments that mimic the structure of the protein to which the toxin ordinarily binds. The toxin then attaches itself to the decoy fragments instead of to the cells protein. This re-routing of the toxin allows neurotransmitters to keep functioning, thus stopping the toxins pathological effects.

The scientists used x-ray techniques at Brookhavens National Synchrotron Light Source (NSLS) to see how the toxin binds to the protein inhibitors. They found that all four decoy proteins are efficient at inhibiting the toxins binding to the cells protein, but one of them in particular is by far the best of any known inhibitors. The scientists next step in this process is to transform the most effective of the four protein fragments into a drug-like molecule before clinical testing is done.

This study represents an impressive collaboration in identifying potential inhibitors of the toxin for therapeutic use, said Colonel George W. Korch, Jr., USAMRIIDs commander. It builds upon the successes we have realized in developing effective next-generation vaccines to protect our citizens against the toxins deadly effects prior to exposure.

The scientists did not work with intact Clostridium botulinum bacteria. Instead, they produced a functional fragment of the neurotoxin protein, which is not toxic. The research is performed in strict compliance with Brookhavens Institutional Biosafety Committee regulations according to standards set by the U.S. Centers for Disease Control and Prevention. Only authorized scientists have access to the laboratory.

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