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Chaperone has identified the residues responsible for DnaK binding in pyrrhocoricin and the pyrrhocoricin binding surface on Escherichia coli DnaK protein. The model is suitable for explaining the activity against all the responsive bacteria with known DnaK sequence, such as Salmonella typhimurium, Haemophilus infleunzae and Agrobacterium tumefaciens. The discovery of the contact side-chain atoms between the pyrrhocoricins and Escherichia coli as well as Haemophilus influenzae DnaK is currently in progress at Chaperone. When this process is complete Chaperone can design pyrrhocoricin analogs that kill currently non-sensitive bacteria, including the most feared Staphylococcus aureus, as well as Streptococcus pneumoniae, Streptococcus pyogenes, Haemophilus ducreyi, Helicobacter pylori, or Enterococcus feacalis, just to name a few. From the point of view of biological warfare, the DnaK sequences of the Category A bacterial pathogens Yersinia pestis and Francisella tularensis are known, and it is very likely that those of Bacillus anthracis and Clostridium botulinum will be published in the very near future.

The sequences of prokaryotic and eukaryotic DnaK/Hsp70 molecules in the multihelical lid region are remarkably different. Future applications of the species-specific inhibition of chaperone-assisted protein folding include the control not only of bacteria, but also fungi, parasites, and insects.

Because higher organisms have multiple copies of the Hsp70 proteins this appears to be a more complex problem, although the Hsp70 sequences in the binding region of a given animal are remarkably similar. Chaperone Intellectual Property covers all biocides that kill organisms by preventing DnaK/Hsp70-assisted protein folding. This also includes the screening of suitable compounds developed elsewhere for binding to the D-E helix region of Hsp70 proteins, and having antibacterial, antifungal, anti-parasitic or insecticide activities.