Quitting smoking is tough, but researchers may have found the key to achieving success in a bacterial enzyme.
Current anti-smoking treatments have been shown to fail in at least 80 to 90 percent of smokers. In a study published in the Journal of the American Chemical Society, researchers explored the use of an enzyme known as NicA2 derived from Pseudomonas putida, a bacterium that consumes nicotine as its only source of nitrogen and carbon, as an alternative. Based on their research, they found that the enzyme can be recreated in the lab and feature a number of characteristics promising for drug development.
The idea is that NicA2 can seek out nicotine as well as destroy it before it gets to the brain, depriving a smoker trying to quit of the "reward" triggered by nicotine which leads to a relapse into smoking. The researchers have been working for over 30 years to create a treatment like that but it was only recently that they stumbled upon NicA2.
Kim D. Janda, one of the authors for the study, said their research is still in the early phases of drug development but their work has shown that the enzyme contains the right properties for their intended goal of creating a new anti-smoking treatment.
To test the enzyme for potential usefulness, the researchers combined mice blood serum first with a nicotine dose equivalent to what a cigarette would have. When NicA2 was added to the mix, the half-life for nicotine went from between two and three hours to between 9 and 15 minutes. With some chemical modifications, the enzyme's dose could be increased, further reducing the compound's half-life so that it doesn't even reach the brain.
Further tests showed the enzyme has the ability to stay stable for over three weeks in the lab at 98 degrees Fahrenheit and doesn't produce toxic metabolites when nicotine is degraded. According to Janda, their next step is to alter the bacterial makeup of NicA2 to mitigate possible immune liabilities and improve stability to allow for a single injection that can last up to a month, making the most out of the enzyme's therapeutic potential.
The study was supported by the Skaggs Institute for Chemical Biology at The Scripps Research Institute. Other authors include Song Xue and Joel E. Schlosburg.
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