The researchers used the three-dimensional molecular structure of an antibacterial peptide: Uperin 3.5,
Researchers have found that the peptideself-assembles into a unique fibrous structure, which, through a complex mechanism of structural adaptation, can change its shape in the presence of bacteria in order to protect the toad from infections.
Antibacterial fibrils on toad skin area sign of neurodegenerative diseases such as Alzheimer's and Parkinson's. They were previously thought to be pathogenic, but it has recently been discovered that some amyloid fibrils may benefit organisms. For example, some bacteria produce such fibrils to fight against human immune cells.
The data obtained indicate that the antibacterial peptide secreted on the toad's skin can be activated in the presence of bacteria.
This is the toad's complex defense mechanism, caused by the attacking bacteria themselves. This is a unique example of evolutionary design.
Meital Landau, lead author of this study
The researchers hope their discovery will lead to medical and technological developments based on the peptide.
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