An increasing number of bacterial pathogens are resistant to antibiotics. The most dangerous of of them have a common
Now researchers have been able to figure out its mechanismactions. Its shape imitates a special three-dimensional structure. It is usually found only in proteins produced by bacteria as building blocks for their outer membrane. The structure is the “key” for inserting proteins into the outer shell at specific locations. Darobactin is a copy of this key. However, it cannot penetrate the bacteria, but simply blocks the “keyhole” from the outside. As a result, the transport of bacterial membrane components is hampered, and they die.
Similar mechanisms are already known in microbiology and are used by other drugs. However darobactin is larger than most drugs and cannot penetrate bacterial entry ports.
It turned out that bacteriaA mutation in the BamA protein gene is responsible for the formation of the outer membrane. Darobactin attacks the Achilles heel of pathogens. It binds directly to the most important part of the protein, the so-called backbone atoms. Because these atoms hold the protein together and determine its shape, they are almost impossible to change (change is a common way for bacteria to fend off a new antibiotic. In fact, darobactin remained effective against all the pathogens for which Hiller and his team conducted laboratory tests. mimicking resistance. In other words, the pathogens failed to change the “broken lock.”
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