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Start-Up Licenses Founder’s Research for Resistant Bacteria

Bacteria growing in petri dishes

(Centers for Disease Control and Prevention)

22 December 2015. A biotechnology company spun-off from University of California in San Diego is licensing technology from the university to develop treatments for bacterial infections now becoming resistant to conventional antibiotics. Financial terms of the licensing agreement between UC-San Diego and Forge Therapeutics were not disclosed.

Forge Therapeutics, also in San Diego, is licensing research from the lab of its scientific founder Seth Cohen, a professor of biochemistry. Cohen and colleagues study metalloproteins, which as the name implies, are enzymes with metallic ions in their chemistry. A number of metalloproteins are associated with a range of diseases, from heart disease and cancer to infections. The lab’s agenda includes study of metalloprotein inhibitors that can be developed into therapies for conditions related to these enzymes.

The license covers Cohen’s research on inhibitors of LpxC, a zinc-based metalloprotein enzyme found primarily on the outer membrane layer of gram-negative bacteria, including dangerous drug-resistant strains of Acinetobacter, Pseudomonas aeruginosa, and E. coli. “Gram” refers to a classification for bacteria where the microbes either retain (gram-positive) or shed (gram-negative) a test stain on their protective cell coatings.

Centers for Disease Control and Prevention says each year some 2 million people in the U.S. become infected with bacteria that are resistant to antibiotics, resulting in at least 23,000 deaths. Gram-negative bacteria are associated with infections such as pneumonia, bloodstream infections, wound, and surgical site infections.

LpxC is considered a promising target for new types of antibiotics, since it’s found largely in gram-negative bacteria and there’s no comparable enzyme in human chemistry. So far, there are no also approved drugs addressing LpxC. Small-molecule compounds currently being tested against LpxC, says the company, bind with the zinc in the enzyme, but are not easily absorbed into the blood stream and can lead to toxic byproducts when metabolized.

Forge Therapeutics says its LpxC inhibitors use a different process for attacking the enzymes. The company’s technology is based on inorganic compounds that address the zinc and other metals in metalloproteins, and break the components connecting the enzyme’s molecular structure. In tests of infections with lab animals, says Forge, its inorganic LpxC inhibitors are shown to be potent, well-tolerated, and effective.

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