New Study Creates Mutant Cocaine-Eating Enzyme

By John Lavitt 07/17/14

The enzyme can potentially be a powerful tool in treating cocaine addiction.

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Living in the dirt under coca plants in South American fields, a local bacteria is powered by an enzyme that actually eats cocaine. The enzyme breaks down quickly when exposed to body temperature so it has never been used to treat human overdoses or cocaine addiction.

A research team at the College of Pharmacy at the University of Kentucky has developed a mutant version of the enzyme which thrives at higher temperatures. The new mutant enzyme thrives to the point that its appetite for cocaine is doubled as well, making it twice as effective as a potential treatment option.

As the scientists explain in their published results, the version of cocaine esterase greatly improves both functioning and stability. Scientists have been investigating ways to harness cocaine esterase's drug-chugging power for therapeutic use, but the 12-minute half-life of the naturally occurring enzyme at human body temperatures proved a tough obstacle to overcome. Researchers at the University of Kentucky previously created an improved enzyme able to withstand body temperatures for 12 hours that already has made its way to clinical trials.

The new mutant enzyme is a huge step beyond that first prototype because it can survive over 100 days at body temperatures while dismantling and ingesting cocaine at a much faster rate. The goal of the research team is to engineer a more valuable therapeutic enzyme for cocaine abuse treatment. Such genetic engineering aims to simultaneously improve both the stability and function to make the enzyme feasible for rational protein drug design.

The team built a computer model of the naturally occurring enzyme, then simulated a high-temperature environment to see which part of the structure failed first. Once they determined the weak points, the research team sought genetic designs and adaptations to improve the survival structure without affecting the enzyme's functionality. In fact, rather than negatively affecting the enzyme’s functionality, the mutant version actually improved on it.

According to the research paper, the modified enzyme fully protected mice from lethal doses of cocaine for at least three days. At this point, the current mutant enzyme in clinical trails could be useful both as a short-term antidote, but not necessarily as a long-term addiction-fighting therapy. If the stability of the current development can be developed into an effective drug therapy, a long-term answer for cocaine addiction could be the incredible result.

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Growing up in Manhattan as a stutterer, John Lavitt discovered that writing was the best way to express himself when the words would not come. After graduating with honors from Brown University, he lived on the Greek island of Patmos, studying with his mentor, the late American poet Robert Lax. As a writer, John’s published work includes three articles in Chicken Soup For The Soul volumes and poems in multiple poetry journals and compilations. Active in recovery, John has been the Treatment Professional News Editor for The Fix. Since 2015, he has published over 500 articles on the addiction and recovery news website. Today, he lives in Los Angeles, trying his best to be happy and creative. Find John on Facebook, Twitter, and LinkedIn.