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Drug aimed at 2 bioterror agents blocks live viral infection, Weill Cornell team reports
Date:12/19/2007

their particular shapes prevent 'doors' in the viral 'fusion protein' from closing as they should. The parainfluenza peptide's shape simply makes it a better door jamb," Dr. Porotto said.

Much of this research is modeled on insights gained from two decades of investigation into another lethal virus, HIV. In fact, T-20, or Fuzeon -- one of the earliest effective HIV-suppressing drugs -- acts on a similar principle to block that virus' entry into cells.

The next step, according to the researchers, is to use what they've learned to design even more effective peptides that should work even better.

"However, one issue with peptides is that you have to be concerned about how long they are going to last in the bloodstream," Dr. Moscona says. "So, we are also developing methods of sustained-release -- for example, encasing the peptide in a polymer pellet that would be injected under the skin. The pellet would then release the drug slowly over the course of a week. That could form a viable method suitable for stockpiling," she says.


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Contact: Andrew Klein
ank2017@med.cornell.edu
212-821-0560
New York- Presbyterian Hospital/Weill Cornell Medical Center/Weill Cornell Medical College
Source:Eurekalert

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