A team of scientists from The Scripps Research Institute (TSRI) have discovered a bacterial enzyme that could “eat” nicotine, and could probably reduce the risk of smoking addiction and relapse. Basically, it could be compared to the “Pac-Man effect”.
Enzymes are compounds produced by living organisms, that function as biochemical catalysts. A catalyst, roughly put, is a chemical substance that precipitates a process, one that modifies and increases the rate of a reaction, without being affected meanwhile.
This particular enzyme, functioning as a weapon against smoking, is called NicA2. It is a bacterial enzyme which prevents nicotine from reaching the brain, which diminishes the effect of (heavy) smoking and relapses.
Kim Janda, study author, chemistry professor and member of the Skaggs Institute for Chemical Biology at TSRI, explained that the research was in the early stage of development. However, the results are promising and goal-oriented.
The bacterial enzyme has demonstrated significant efficacy in anti-smoking therapy. The enzyme could work as an alternative to traditional smoking cessation aids, which had failed in almost 90 percent of smokers.
The TSRI team discovered the NicA2 from the bacteria Pseudomonas putida; they had been trying to come up with a solution that would enable people to fight nicotine addiction for approximately 30 years now. Pseudomonas putida was initially isolated from soil in a tobacco field and it seems that nicotine is metabolized with the help of the NicA2 enzyme.
Janda also associated the NicA2 enzyme to the popular video game protagonist – the little Pac-Man. He says it goes along and eats nicotine.
It has been revealed, thorough extensive analysis and lab-conducted investigations, that a relatively high dose of the enzyme, including a few chemical modifications, could reduce the half-life of nicotine and stop it from reaching the brain. The scientific team had combined a blood component with a dose of nicotine equal to one cigarette, and when the enzyme was added, the half-life of the nicotine had diminished from 2-3 hours to 9 to 15 minutes.
The researchers then went on to study whether the enzyme could be turned into a drug that would help smokers. Janda concluded that it was rather remarkable that the enzyme was stable in a laboratory for over three weeks at 98 degrees Fahrenheit. Moreover, no toxic metabolites were identified as left-overs, after the bacterial enzyme had eaten the nicotine.
Janda also reported that the enzyme is to be chemically altered, so that it wouldn’t produce immune problems and in order to maximize its therapeutic effects.
Song Xue, TSRI graduate and co-author of the study, reported that the enzyme was quite stable in serum, which was important for a therapeutic candidate. Also, Song Xue hopes that the serum stability can be improved in time, so that a single injection may last up to a month.
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