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Chaperone Technologies: Preventing the Rise of a “Superbug”

For years, scientists have warned that the overuse of antibiotics is leading to more drug-resistant pathogens. Such resistant bacteria-or “superbugs”-have long posed significant danger in hospitals and could present a frightening bio-terrorism scenario as well.

Chaperone

Bacterial resistance toward many conventional antibiotics has increased from zero in the early 1950s to almost 100% by now, says Chaperone Technologies. Their new compounds are designed to attack such resistant bacteria.

“If someone is going to weaponize Category A biowarfare pathogens such as plague or tularemia, they are unfortunately likely going to engineer a resistant strain,” says Kenneth Kovan, CEO of Scranton-based Chaperone Technologies, Inc. “We are designing compounds that kill these and related families of bacteria that don’t respond well to current antimicrobial treatments.”

Chaperone, who through a unique collaborative arrangement and helping hand from BFTP has its lab based at Lackawanna College, just received a $1 million directed appropriation from the U.S. Department of Defense to further develop their technology to target selected “Category A” biowarfare pathogens.

Developing Treatment for Worst Pathogens

“We’ve already shown through previous tests with the U.S. Army that our compounds can kill selected Category A pathogens,” Kovan says. “This new project will enable us to significantly advance our program to fully develop a treatment for some of the worst of these pathogens.”

While some broad spectrum antibiotics are currently indicated for selected Category A biowarfare pathogens, concern is growing that the widespread and aggressive usage of key antibiotics such as ciprofloxacin will accelerate the development of resistant strains of more common bacteria.

Chaperone’s unique approach involves the creation of novel compounds that bind to a bacteria’s DnaK-a class of intracellular bacterial structures whose role is to correct misshapen proteins.

DnaK Controls Protein Folding

“A process called ‘protein folding’ is critical to the lifecycle of every living being,” says Dr. Michael Sturgess, director of chemistry for Chaperone. “One role of DnaK is to control protein folding. Our compounds bind to the DnaK and interrupt the process, thus killing the target organism.”

Some of Chaperone’s work continues to take place at the University of Scranton, a place the company called home when they first moved to the region. BFTP funding and networking assistance helped the company first set up shop at the school’s acclaimed Institute of Molecular Biology and Medicine (IMBM).

Then as Chaperone outgrew its IMBM space, BFTP connected Kovan with Lackawanna College, which, as a commitment to their own bio-science efforts, carved out a new lab for Chaperone. The company and college continue to collaborate on grant opportunities and other projects.

A Direct Impact on Saving Lives

“We would not be where we are today-literally and figuratively-without BFTP,” says Kovan, whose company has received over $300,000 in BFTP seed funding since 2004. “They have certainly fulfilled their role of identifying a promising technology and providing the resources to make it happen.”

In addition to seed money and other support from BFTP, Chaperone has received an investment from Innovation Philadelphia, and most recently a $100,000 investment from the Life Sciences Greenhouse of Central Pennsylvania.

Chaperone’s discoveries won’t hit the market for a few years, but Kovan is already looking ahead. “We like to think we’re going to have a direct impact on saving lives, be it a soldier on the battlefield or someone going in for surgery,” he says. “That’s a great motivator.”

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This article was featured in
Keynotes April, 2006
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