Scientists are building tiny, molecular drill bits that kill bacteria by bursting through their protective cell walls, in response to drug-resistant superbugs that send millions of people to hospitals around the world.
Scientists are building tiny, "molecular drill bits" that kill bacteria by bursting through their protective cell walls, in response to drug-resistant "superbugs" that send millions of people to hospitals around the world. They presented some of the latest developments on these drill bits, better known to scientists as antimicrobial peptides (AMPs), at the 247th National Meeting & Exposition of the American Chemical Society (ACS), the world's largest scientific society.
The meeting, which features more than 10,000 scientific reports across disciplines from energy to medicine, continues here through Thursday.
One of the researchers in the search for new ways to beat pathogenic bacteria is Georges Belfort, Ph.D. He and his team have been searching for a new therapy against the bacteria that cause tuberculosis (TB). It's a well-known, treatable disease, but resistant strains are cropping up. The World Health Organization estimates that about 170,000 people died from multidrug-resistant TB in 2012.
"If the bacteria build resistance to all current treatments, you're dead in the water," said Belfort, who is at Rensselaer Polytechnic Institute.
To avoid this dire scenario, scientists are developing creative ways to battle the disease. In ongoing research, Belfort's group together with his wife, Marlene Belfort, and her group at the University at Albany are trying to dismantle bacteria from within. They also decided to attack it from the outside.
In their search for a way to do this, they came upon AMPs. Although these naturally occurring, short strings of amino acids are not new — all classes of organisms from humans to bacteria produce them as part of their natural defense strategy — the fight against drug-resistant pathogens has heightened attention on these protective molecules.
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Intrigued by their potential, Belfort scoured recent work on the peptides and discovered a database filtering technique developed by another group, reported in 2012. It's a kind of design-your-own-AMP model.
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Belfort's team is now focused on improving their designs and understanding exactly how AMPs work. The group is also developing a laboratory test that will allow them to tell within hours rather than weeks if an AMP is working against Mycobacterium tuberculosis.
If developed into pharmaceuticals, AMPs could have the additional benefit of overcoming the very challenge they're designed to meet: drug-resistance. AMPs attack bacteria's walls, or cell membranes, which have been conserved through a long history of evolution.
"It's going to be much more difficult for a bacterium that's been around for millions of years to reconfigure its membrane," Belfort said. "That's the core protective structure that has helped it survive this long."
Source-Eurekalert