It seems a near certainty that future research, and researchers, will find small-molecule compounds that bind more elegantly to this pocket, than ibuprofen does. Even so, it is exciting that at least one small molecule -- one well-understood, and well-tolerated by humans -- binds to this pocket (and is a well vetted, common pain-reliever). [Regular readers here know that Merck's vaccine is highly effective, but reliable treatments for acute cases don't yet exist.]
Indeed, I'd say it's worth a read of the whole article in Nature, via this summary at Chemical and Engineering News -- and here's a bit of it:
. . . .Researchers led by Oxford University’s David Stuart solved the structure of the virus glycoprotein to a resolution of 2.2 Å in complex with two different molecules that scientists have shown can reduce infection in rodents: ibuprofen and the chemotherapy drug toremifene. . . .
When the Ebola virus infects a host cell, the first thing it does is attach itself to the cell using a glycoprotein. A newly obtained structure of that glycoprotein — the highest resolution one to date — now reveals a vulnerability in the virus’s infection machinery. Given the lack of approved therapies to combat the virus, this work gives medicinal chemists a weak point to target as they try to design molecules that stop Ebola’s deadly spread. . . .
Stuart’s team found that both chemicals bind in a buried pocket of the virus glycoprotein. The binding of these chemicals likely pushes the glycoprotein prematurely into a state where it can’t infect host cells, Stuart says. . . .
It is often the simplest answers that are the most elegant. We will hope to be back much later on the Fourth, with updated news from Jupiter -- if all the Universe's forces align on this coming 2016 Independence Day evening. Smile. . . .
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