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The structure of the first cannabinoid receptor revealed

The structure of the first cannabinoid receptor revealed
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New research of importance, the structure of the main cannabinoid receptor (CB1) is finally revealed

Scientists have discovered the molecular structure of the cannabinoid receptor 1 (CB1) known to interact with THC. The discovery will help better understand and better use medical marijuana. And surely to do away with dangerous products, such as synthetic "marijuana"

Discovery of NIDA

The National Institute on Drug Abuse (NIDA) supports most of the world's research on the health aspects of drug use and addiction. NIDA is known for not supporting pro-cannabis research. Yet in this case, she surprises by funding the National Institutes of Health (NIH) in a new study detailing the human cannabinoid receptor, the CB1. The results provide key insights on how natural cannabinoids. Of which THC (tetrahydrocannabinol) and synthetic interact with the CB1 receptor.

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“Cannabinoids can produce very different results, depending on how they bind to the CB1 receptor,” said the Director of NIDA,  Nora D. Volkow, MD - "Understanding how these chemicals bind to the CB1 receptor will help design new drugs and provide insight into the therapeutic promise of the human body's cannabinoid system."

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Nora D. Volkow

According to the authors, the study published in Cell paves the way for the development of CB1 pharmaceutical products targeting the next generation.

The “freeze” of CB1

It was very difficult to study the CB1 receptor, given its structure found to be unstable (in motion), "which is particularly surprising because CB1 is so common" states Raymon Stevens, chemist at the University of Southern California.

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Artist's vision of the molecular structure of the CB1 receptor: AM6538 is represented by the color orange, and THC by the color yellow (credits Yekaterina Kadyshevskaya,)

Researchers have developed a special molecule that "freezes" receptors long enough to glimpse its molecular structure. The chemical AM6538 was used to crystallize and "inactivate" the CB1 receptor; therefore they were able to calculate the three-dimensional structure of the CB1 complex (+ AM6538). This by crystallography and glimpsing how THC and other molecules interact with the receptor.

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Alexandros Makriyannis

 “We weren't expecting such a complex structure. »Declares Alexandros Makriyannis the director of the Center for Drug Discovery, Northeastern University, Boston, and co-author of the study.

New discoveries possible

Knowing the structure of CB1 provides new foundations for future research on marijuana and its related effects.

"We found that the CB1 receptor consists of several sub-pockets and channels." Said Alexandros Makriyannis. “This complex structure allows chemists to design compounds that specifically target the various portions of the receptor to produce desired effects. "

The model was also used to calculate the duration of cannabinoids bound to the CB1 receptor. In addition, imaging provides clues to mechanisms by which certain chemicals produce more lasting effects.

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“Think of the receptor as an array,” says co-author Zhi-Jie Liu, a molecular biologist at ShanghaiTech University. CB1 is connected to wires which can each cause relief in pain, depression etc. We can design specific molecules and drugs that could, for example, suppress appetite without causing depression.

The death knell for "synthetic cannabis

The team also received a grant from the NIH to work on direct observation of the dangerous molecules contained in synthetic “cannabis”. This is to determine how the receiver turns on and off. What makes the specificity of synthetic products like K2 and and Spice.

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Synthetic marijuana like K2 or Spice or other synthetic products interact dangerously with the CB1, and can cause serious and even fatal reactions. It goes without saying that the results to come will spell the end for products based on synthetic “marijuana”. This will definitely rehabilitate the natural THC present in the cannabis plant.

Tags : ReceiverSearch
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