Those who tried to quit smoking but always fail may soon find help from an unusual source, a bacterium.
Researchers from The Scripps Research Institute (TSRI) have discovered a particular enzyme from bacteria that feed on nicotine, which then could help smokers quit the bad habit before the addictive substance reaches the brain, as reported in Times of San Diego.
The new study, which appeared in the Journal of the American Chemical Society on Thursday, demonstrates how the enzyme can potentially be turned into alternative smoking cessation aids, which fail most of the time.
The enzyme in question is from Pseudomonas putida, a bacterium that is isolated from soil in tobacco fields.
P. putida chomps on nicotine as its primary source of nitrogen and carbon. The not-for-profit research institute showed that its enzyme, dubbed NicA2, can be replicated in laboratories without compromising its potency, consequently making it a possible candidate for the drug industry.
"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 Professor Kim Janda of the Skaggs Institute for Chemical Biology at TSRI.
According to Drug Discovery & Development news report, the researchers first mixed mice serum with nicotine levels equal to one stick of cigarette.
When the bacterial enzyme was introduced, the half-life for nicotine was reduced from two to three hours to nine to 15 minutes.
According to Janda, if a higher dose of the enzyme is supplied and topped with a few tweaks to its chemical composition, it could potentially induce a much better reduction to nicotine's half-life.
He also mentioned that the results were encouraging since the enzyme remained stable in the lab even after more than three weeks in a 98-degree Fahrenheit environment.
More importantly, researchers found that the enzyme did not produce any toxic metabolites when it broke down nicotine.
The next step for the team is to make some changes on the bacterial makeup of NicA2 to exploit more of its therapeutic properties.
