Whether man-made or naturally produced, phosphonates and phosphinates are structurally similar to other compounds used by enzymes in nature. They sometimes bind to the same enzymes and thus can inhibit ordinary cellular processes in bacteria or other organisms. This makes them attractive candidates for the development of new antibiotics, said van der Donk, a principal investigator on the study with Metcalf and biochemistry professor Satish Nair.
Understanding how bacteria synthesize these compounds also enables the scientists to predict how bacteria might develop resistance to any new drugs that are developed, he said.
"Knowing how a compound is made may allow you to make an analog that can overcome that resistance," van der Donk said. "That's the game that's been played with penicillin for the last 40 years. Every time a bacterial strain becomes resistant to one penicillin, scientists tinker with the structure so that the organism is susceptible again."
The researchers hope the new findings will spur the development of much smaller, cheaper and more efficient synthetic catalysts that can also sever C-C bonds in one step.
"Every time we find something new in nature it's an inspiration to see if we can copy that reactivity with a small molecule," van der Donk said.
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| Contact: Diana Yates, Life Sciences Editor diya@illinois.edu 217-333-5802 University of Illinois at Urbana-Champaign Source:Eurekalert |