Our pre-clinical development programs are focused on therapeutic areas where we believe our technology can generate new medicines from pharmaceutically relevant, and oftentimes clinically established, therapeutic peptides and proteins. Without the benefit of our technology many of these peptides and proteins would have numerous shortcomings, including, difficulties with expression, purification, manufacture, bioavailability, and the need for frequent dosing which can result in unwanted side effects. Our current lead programs are centered around medically relevant hormones, enzymes and natural and proprietary peptides.

Diabetes and Metabolism

As an extension of our clinical efforts with Albulin-G, programs at CoGenesys include development of long-acting glucagon antagonists and GLP-1 receptor agonists for the treatment of type 1 and type 2 diabetes and associated weight gain. These efforts include use of multiple fusion-protein technologies and expression systems with the aim of addressing the need for extended bioavailability, infrequent dosing and low cost of goods.

Enzyme Addition and Replacement Programs

Butyrylcholinesterase

CoGenesys is developing a long-acting Butyrylcholinesterase (BChE) derivative for the detoxification and treatment of cocaine abuse. BChE is a low abundance serine hydrolase that can hydrolyze ester containing drugs such as cocaine. It is known that the tetrameric form of the enzyme can be used to protect rodents from the toxic effects of cocaine. Difficulties in expression and purification of both native and recombinant BChE have hampered drug development efforts. Studies at CoGenesys have focused on development of a long-acting monomeric albuminated form of the enzyme that can be produced in sufficient quantities to enable commercial development. Lead molecules have advanced to the stage of evaluation in rodent models of cocaine toxicity.

Phenylalanine Hydroxylase

Phenylalanine Hydroxylase (PheOH) is an iron- and tetrahydropterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. Mutations in the PheOH gene result in the metabolic disease known as Phenylketonuria (PKU). Without dietary restriction of phenylalanine, children with PKU will develop profound and irreversible mental retardation. Because of difficulties in production of recombinant PheOH, enzyme replacement therapies remain non-existent. Our efforts in this area include generation of modified forms of PheOH that with the appropriate fusion protein partner will result in a recombinant enzyme that has significant extended bioavailability and can be produced at yields required to enable development of new treatment options for this disease.