New technologies that make the dye from a single-celled organism can be used to make photocatalysis-based photocatalysers for a variety of applications, from dyeing clothing to cleaning up polluted rivers.The U.S. Food and Drug Administration's (FDA) Office of Technology Development (OSTD) said the new technology will allow researchers to easily make the pigment from a group of bacteria called Bac...
With a lot of the new technologies, you might think it’s easier to make photocatalytic chemicals from scratch, but there’s still a long way to go.
For example, the photocatalysis technology used in the latest batch of the Nobel Prize-winning anthraquinones, which was released in May, is a completely new class of chemical that uses the reactions between amino acids and sugars to produce a new kind of protein.
But even though anthraquins are made with enzymes, the process isn’t quite as simple as you might expect.
“It’s actually quite complicated,” says Paul Vickers, an associate professor of chemistry at Duke University.
In fact, there are more than 100 different enzymes in anthraqinone, so it can take several weeks to make them all work.
“There’s so much complexity in this process that it’s quite challenging to make it work,” Vickers says.
Vickers is not alone.
He’s been studying the chemistry of anthraqiens since 2009.
“You can do the same thing with all of these other compounds,” says Vickers.
He is not the only one looking at the chemistry behind the chemistry.
In March, the European Chemical Society (ECS) published a new study of anthrax and anthraqueins that looked at how the chemistry works in a way that makes it easy to make the new compounds.
In this paper, the ECS researchers say the anthraqqinones have two main properties that make them easy to produce: they’re relatively simple and easy to manufacture, and they can be synthesized in the lab.
“They’re very promising,” says ECS chemist Jürgen Schumacher, a co-author on the paper.
The new compounds were discovered in the 1970s in the laboratories of Charles E. and Martha M. Trombley of the University of Maryland, but they weren’t known to be very good photocatalysis, and some of them were even toxic.
That changed in 2005 when a group of scientists led by Richard J. Higgs of the U.S. Department of Energy found that the anthrax was made by using two enzymes that bind to the anthrqqinone’s amino acids, turning them into a protein.
“That’s when the whole world caught on that we could make these,” Higgs says.
This discovery has given scientists a new tool to explore the chemistry and biology of the anthracinones.
And because of the nature of the enzymes, they are relatively easy to isolate and use in their own labs, Vickers and Schumachers say.
“When we put them into the laboratory, we get a really good picture of how these enzymes work,” Schumchers says.
So far, the researchers have found that about half of the materials produced by anthraqs have been chemically stable.
They have been able to produce more than 80 percent of the compounds they tested, and all the compounds that are being tested have been stable at room temperature.
“The problem is that we don’t have any laboratory facilities to test them in, so they’re essentially being made in a lab,” Schummachers says.
But this is still very promising.
“We’re very optimistic that we can start to see this in the real world in the next few years,” Vicker says.
That’s because the next step for these researchers is to make their compound, and to try and figure out how to use it to make something that is more stable.
That will be important for scientists looking to make more useful drugs.
For instance, one way to make anthraques is to use them to make pharmaceuticals, such as antifungals.
But there are some drawbacks to using the anthrabiotic compounds in that way.
They aren’t very efficient at making the compounds.
And they don’t produce any antimicrobial activity.
So scientists are looking at ways to improve these compounds.
“This work provides a window into the chemistry that goes into making anthraqlens, but it’s not a perfect window,” Vicks says.
It also leaves us with some questions about the chemistry involved.
Is it really the same chemistry that made anthraqaens?
Are there any different ways of making them?
Does the new chemistry give us a way to improve anthrax therapies?
And, of course, does it actually help us make better anthraqualones?
In other words, is it really safe to make these compounds?
That’s something the Ecs team hopes to answer in the coming months.
They’re working to figure out exactly how these chemicals work, and how to make things that are stable at the lab and don’t affect the human body in ways that are harmful.
They want to find a way of making more anthraquerones in the future.
“I’m optimistic we will get a very useful drug in