BioWorld International Correspondent

OTTAWA, Ontario - Two Kingston, Ontario, companies are collaborating to identify the function of novel cytochrome P450 proteins. Cytochroma Inc. and Molecular Mining Corp. will search for novel genes that will enhance a library of validated molecular targets for drug discovery.

Cytochroma uses genomic information to identify novel cytochrome P450 enzymes and develop therapeutic drugs that act on these enzymes. To date, Cytochroma's drug discovery program has identified modulators of vitamin A and vitamin D metabolism as drug candidates for the treatment of skin diseases, cancer and bone disorders.

Although there likely are more than 100 genes encoding P450 enzymes in the human genome, exploitation of the many specific cytochrome P450s, which play pivotal roles in metabolic processes, has been hampered by lack of knowledge of their structure, their substrate preferences and thus the discovery of compounds that selectively inhibit their action. Core technologies at Cytochroma have been established to investigate metabolic pathways in which P450s participate, as well as to identify cytochrome P450-specific inhibitors using high-throughput screening.

Robert Foldes, president & CEO of Cytochroma, said the companies will leverage their individual strengths to accelerate the development of a pipeline of novel gene targets. Cytochroma already has built the infrastructure and expertise to rapidly identify the function of novel cytochrome P450 proteins and Molecular Mining is using its advanced data mining and modeling platform to assist in this task.

Molecular Mining specializes in the exploration and prediction of biomolecular pathways and complex phenotypes from gene expression, proteomics, SNPs and high-throughput screening data. It has developed its GeneLinker Gold, an entry-level product in a segmented line of gene expression analysis solutions that includes a family of software products. The first report from Molecular Mining has identified hundreds of possible gene sequences with significant homology to cytochrome P450s, it said.

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