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The PSI researchers have developed proteins that attach to the part of the enzyme responsible for the effect on the nerves. The idea: this way the effect is inhibited.
However, to the researchers’ surprise, the opposite happened: the toxic effect started even faster than normal, according to a study published on Monday in the journal ‘Nature Communications’. “We initially thought we had done something wrong,” lead author Oneda Leka said in the PSI statement.
Botulinum toxin A1, Botox for short, became known for its use as a cosmetic aid. However, Botox is also used in therapeutic medicine, as the PSI emphasizes. For example, to treat pain, spasticity or bladder weakness. Even in stomach cancer, Botox is used to block the vagus nerve and thus slow tumor growth.
Botox works by breaking down certain proteins that are important for the transmission of nerve signals. In the research project, the researchers artificially produced small proteins, called DARPin, that were intended to function similarly to antibodies and would attach to the part of the protein responsible for cutting up other proteins.
“In vitro – that is, in the test tube of individual samples – we have also identified a suitable DARPin candidate that inhibits the function of botulinum toxin,” says study leader Richard Kammerer. However, in experiments in the laboratory and later in the muscles of mice, the opposite happened.
The researchers explain this by saying that the DARPin actually destabilizes the toxin in such a way that it is transported more quickly into the interior of the nerve cell.
But this is not bad news, the researchers emphasized: Botox, for example, could relieve pain faster than before. (SDA)
Source:Blick
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