The researchers found that the bacterial enzyme can be recreated in lab settings and possesses a number of promising characteristics for drug development.
“Our research is in the early phase of drug development process, but the study tells us the enzyme has the right properties to eventually become a successful therapeutic,” said one of the researchers Kim Janda, professor of chemistry at The Scripps Research Institute (TSRI) in California.
The new research offers a possible alternative to current smoking cessation aids, which are shown to fail in at least 80 to 90 percent of smokers.
The idea behind an enzyme therapy would be to seek out and destroy nicotine before it reaches the brain — depriving a person of the “reward” of nicotine that can trigger relapse into smoking.
For more than 30 years, Janda and his colleagues have struggled to create such an enzyme in the lab, but they recently ran across a potential enzyme found in nature — NicA2 from the bacteria known as Pseudomonas putida.
It turns out this bacterium — originally isolated from soil in a tobacco field — consumes nicotine as its sole source of carbon and nitrogen.
In the new study, the researchers characterized the bacterial enzyme responsible for nicotine degradation and tested its potential usefulness as a therapeutic.
Importantly, the researchers detected no toxic metabolites produced when the enzyme degraded nicotine in the lab.
“The enzyme is also relatively stable in serum, which is important for a therapeutic candidate,” study first author Song Xue, graduate student at TSRI, said.
The study was published in the Journal of the American Chemical Society.