Analyzing Poppies to Make Better Drugs
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Analyzing poppies to make better drugs
In a paper published in the Journal of Biological Chemistry, the scientists explain how they revealed molecular details of an enzyme class that is central to the synthesis of many widely used pharmaceuticals, including the painkillers codeine and morphine. The team used the Canadian Light Source (CLS) at the University of Saskatchewan and the SLAC National Accelerator Laboratory to better understand how the enzyme behaves, which is crucial for unleashing its potential to make novel medicines.
"Until this study, we didn't know the key structural details of the enzyme. We learned from the structure of the enzyme bound to the product how the methylation reaction locks the product into a certain stereochemistry. It was completely unknown how the enzyme did that before we determined this structure," corresponding author Dr. Kenneth Ng explained.
Stereochemistry is an important concept when it comes to safety and efficacy in drug design. A molecule can have a few different arrangements-similar to how your left hand is a mirror image of your right hand. These arrangements can lead to very different effects.
"There are a lot of classical examples where it can have a big effect," lead author Dean Lang said. "Thalidomide is a famous historical example. When you have it in one stereochemical form it's a good treatment for nausea, but in the opposite stereochemical form it can lead to birth defects."
In this study, the stereoselectivity of the yellow horned poppy's enzyme controls what substrates can interact, the products you will get, and how much medicinal compound you can extract from the plant. Understanding how key enzymes behave can help bioengineers to optimize their drug production and allow researchers to explore new or rare compounds
[...] Dr. Facchini stressed the importance of the hard work done by researchers involved in this study and the strong collaboration between their respective labs. He is hopeful that their research could lead to new, effective drugs in the future.
More information: Dean E. Lang et al. Structure-function studies of tetrahydroprotoberberine N-methyltransferase reveal the molecular basis of stereoselective substrate recognition, Journal of Biological Chemistry (2019). DOI: 10.1074/jbc.RA119.009214
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