The Scripps Research Institute (TSRI) researchers are studying a bacterial enzyme that shows potential in being used to help people stop smoking, a habit associated with increased risks for a range of unwanted health conditions such as cancer and respiratory problems and early death.
The research, which was published in the Journal of the American Chemical Society on Aug. 6, is still in its early phase but it shows that the enzyme can be reproduced in lab setting. It also has a number of characteristics that have potentials for drug development offering hope for a new alternative to currently available smoking cessation aids which do not work for a large percentage of smokers.
Kim Janda, from TSRI, said that their study shows that the enzyme possesses the right properties that could later on become a successful treatment.
The concept behind an enzyme therapy is to find and destroy the nicotine prior to it reaching the brain, which would deprive the smoker of the reward of the chemical which can then help initiate relapse into smoking.
Janda and colleagues sought to create one such enzyme in the lab for over three decades but only recently were they able to encounter a potential enzyme that is found naturally. The enzyme is known as NicA2 and it comes from the bacterium Pseudomonas putida, which consumes nicotine as its only source of nitrogen and carbon.
"The bacterium is like a little Pac-Man," said Janda. "It goes along and eats nicotine."
For their research, Janda and colleagues combined mice blood serum with nicotine, the amount of which is comparable to that found in one cigarette, to test the potential impact of the enzyme on tobacco addiction.
The researchers found that when the enzyme was present, the half-life of the nicotine was reduced to as short as nine minutes from two to three hours. The enzyme was also found to be stable in the lab for over three weeks at 98 degrees Fahrenheit.
NicA2 do not likewise appear to be producing toxin metabolites and is comparatively stable in serum, which makes it potentially viable to be developed as a drug.
"In characterizing the enzyme, a favorable biochemical profile of the enzyme was discovered, making NicA2 a prospective therapeutic candidate," the researchers wrote in their study. "This approach provides a new avenue for the field of nicotine addiction therapy."
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