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Chesapeake PERL To Produce Nerve Agent Bioscavenger For DTRA

C-PERL Will Produce Nerve Agent Bioscavenger Butyrylcholinesterase for Defense Threat Reduction Agency using Proprietary Protein Production System.

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SAVAGE, Md., Oct. 24, 2012 /PRNewswire/ -- Chesapeake PERL has been awarded a contract to develop the human nerve agent bioscavenger butyrylcholinesterase (BChE) as a potential nerve agent countermeasure for the Defense Threat Reduction Agency (DTRA).  The contract will fund development of a recombinant human BChE and its production in C-PERL's PERLXpress high efficiency protein manufacturing system.  C-PERL will collaborate with the US Army Medical Research Institute of Chemical Defense (located on the Aberdeen Proving Grounds, MD) to test the circulatory stability and anti-nerve agent protective efficacy of the recombinant BChE, with the ultimate objective of advancing a product into human clinical trials.

BChE is the lead bioscavenger candidate based on its ability to afford protection over a broad range of highly toxic organophosphorus nerve agents.  It is a natural mammalian blood protein that can be administered either prophylactically or post-exposure, but is normally present at low concentrations in human plasma making it both expensive to produce and severely limited in supply.  DTRA is seeking economical alternative production methods utilizing recombinant technology, and has selected C-PERL for its experience in manufacturing high quality proteins using its highly automated, efficient and cost-effective PERLXpress production system.

Chesapeake PERL is a biological manufacturer specializing in the production of high quality proteins, including glycosylated and lipid-associated proteins, multimeric forms and self-assembling macromolecular structures.  PERLXpress, the Company's proprietary, highly automated in vivo implementation of the Baculovirus Expression Vector System, employs whole insect larvae as mini-bioreactors.  The tissue heterogeneity of the insect bioreactors leads to very high levels of protein expression as well as protein modification and processing that closely resemble native versions of the same proteins, and the system flexibility enables rapid, precisely controlled production from micrograms to tens of grams of protein.

Contact:  Dr. George Buchman - 301-317-9300 x104 -

SOURCE Chesapeake PERL


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