An early-phase study developing a new drug to aid smoking cessation has found that an enzyme made in the lab could digest nicotine before it reaches the brain.
In the Journal of the American Chemical Society, scientists from The Scripps Research Institute (TSRI) report how the enzyme can consume nicotine, indicating the potential to significantly reduce the length of time that nicotine remains in the blood.
The team assessed a protein extracted from Pseudomonas putida bacteria in mouse models. P. putida was originally isolated from a tobacco field and is now known to rely on nicotine as its sole source of carbon and nitrogen. The team isolated the nicotine-degrading enzyme, NicA2, from the bacteria to establish whether this protein was stable and whether the process would continue once the protein was isolated.
The results showed that the protein reduced the half-life of the nicotine from one cigarette from 2–3 hours to 9–15 minutes. The team found no evidence of any negative physical or behavioural effects of the enzyme on the mice and, at this stage, the by-products from the process of breaking down the nicotine do not appear to be toxic.
The authors state that further studies are necessary, particularly with regard to any human immune-response to the protein.