SOURCE: Biolex Therapeutics

March 01, 2007 09:00 ET

Biolex Therapeutics Researchers Present Preclinical Data for Direct-Acting Thrombolytic BLX-155 at Scientific Conference

First Protein Expression System to Produce Commercially Viable Levels of Full-Length Recombinant Plasmin

PITTSBORO, NC -- (MARKET WIRE) -- March 1, 2007 -- Biolex Therapeutics researchers presented data at the 51st Annual Congress of the German Society of Thrombosis and Haemostasis Research in Dresden, Germany demonstrating the successful production of full-length recombinant human plasmin (BLX-155) using the Company's proprietary LEX System(SM), a milestone never achieved at commercially viable levels with any existing protein expression system. Plasmin is the key enzyme in the human body that dissolves the fibrin component of blood clots. The development of a recombinant version of plasmin provides a potential best-in-class product profile for the Company's BLX-155 drug candidate.

Market Need for Recombinant Plasmin (BLX-155)

BLX-155, a full-length recombinant plasmin, is a direct-acting thrombolytic agent designed to dissolve blood clots in patients with acute peripheral arterial disease, deep vein thrombosis, and catheter occlusion, for whom safe and effective therapy remains a substantial unmet medical need.

Acute peripheral arterial occlusive disease (aPAO) is a condition caused by a sudden reduction in blood flow to the extremities due to progressive clot accumulation around an atherosclerotic plaque in the diseased artery. More than 100,000 cases of aPAO are reported annually in the United States and the disease is a significant cause of nerve and muscle damage and, in severe cases, amputation or death. Although no drugs are currently approved for the treatment of aPAO, patients are typically treated with a combination of the use of catheters, the delivery of plasminogen activators, such as tPA, to the site of the clot, and surgery. Plasminogen activators have been relatively unsuccessful in dissolution of the long, older and more compacted blood clots associated with aPAO. In addition, treatment of aPAO with plasminogen activators often require intensive care stays of 24 to 36 hours and may result in bleeding complications at sites remote from the clot.

Research suggests that intact, full-length recombinant human plasmin is ideal for the treatment of blood clots, as it combines the potential for superior clot dissolution with substantial safety advantages. The five kringle domains of natural plasmin enable a high affinity and specificity for binding to the fibrin component of blood clots. Researchers believe that plasmin's high affinity to fibrin may result in a therapy that is more effective than other direct thrombolytics in development such as alfimeprase and truncated forms of plasmin, each of which lack the five kringle domains of full-length plasmin. Additionally, as a native protein, plasmin is regulated by a number of inhibitors within the body that exist in high quantities and serve to rapidly inactivate any plasmin that circulates beyond the immediate site of the clot. This safety mechanism may decrease the risk of bleeding complications associated with the therapeutic administration of plasminogen activators and alfimeprase. The combination of plasmin's high affinity to fibrin and the presence of high level of circulating plasmin inhibitors provides protection from bleeding complications and may result in a therapy with a higher therapeutic index than other direct thrombolytics.

Presentation at Society of Thrombosis and Haemostasis Research

In a presentation entitled "Recombinant Plasmin from Lemna Minor - Purification, Characterization and In Vitro Comparison to Human-Plasma Derived Plasmin," researchers presented data demonstrating that BLX-155, recombinant plasmin produced using the LEX System, is indistinguishable from human plasma-derived plasmin in characterization and activity. These results are significant, due to the fact that the production of full-length recombinant human plasmin at commercially viable levels has only been reported using the LEX System. The limitations of existing production systems have resulted in the production of truncated versions of plasmin that lack the full five kringle domains of native plasmin and therefore lack the natural affinity for fibrin. As a result of these limitations full-length plasmin previously could only be derived from human donor plasma, but this source is limited and carries the potential for transmitting human pathogens. The development of BLX-155 using the LEX System allows exploitation of the natural binding, efficacy and safety advantages of natural plasmin without the limitations or risks associated with truncated plasmin, plasma-derived plasmin, plasminogen activators, or alfimeprase.

"We are excited with the results presented at this conference, which once again confirm the capability of the LEX System to produce hard-to-make proteins and to provide key advantages over existing production systems," said Mr. Jan Turek, Biolex's Chief Executive Officer. "We expect to file an IND to commence a Phase 1 clinical study of BLX-155 at the end of this year. The advancement of this product into clinical trials is in line with our strategy to identify and commercialize proprietary products that rely upon known mechanisms of action to provide a reduced risk profile while targeting large, proven pharmaceutical markets."

BLX-155 is an investigational therapeutic candidate and has not been approved for sale by the United States Food and Drug Administration or any international regulatory agency.

About Biolex Therapeutics

Biolex Therapeutics is developing and commercializing therapeutic proteins based on its proprietary LEX System(SM), an expression system that enables the production, development and commercialization of hard-to-make proteins and the optimization of monoclonal antibodies. The Company is developing a proprietary pipeline of products that rely upon known mechanisms of action to provide a reduced risk profile while targeting large, proven pharmaceutical markets. Biolex's lead candidate, Locteron™, is in Phase 2 clinical trials as a best-in-class controlled-release interferon alfa for the treatment of hepatitis C. The Company's second product candidate, BLX-155, is a direct-acting thrombolytic, designed to break up clots in certain diseases such as acute peripheral arterial disease, catheter occlusion and deep vein thrombosis. In addition, the unique capabilities of the LEX System have led to collaborations with Centocor, Medarex and other leading pharmaceutical/biotech companies. Biolex is a venture-capital-backed company located in the Research Triangle region of North Carolina, United States. For additional information, please visit Biolex's web site at www.biolex.com.

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