The researchers used the three-dimensional molecular structure of an antibacterial peptide: uperin 3.5.
Researchers discovered that the peptideself-assembles into a unique fibrous structure that, through a complex mechanism of structural adaptation, can change its shape in the presence of bacteria to protect the toad from infection.
Antibacterial fibrils on toad skin area sign of neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Previously thought to be pathogenic, it has recently been discovered that some amyloid fibrils may provide benefits to organisms. For example, some bacteria produce such fibrils to fight human immune cells.
The findings suggest that an antibacterial peptide secreted on the toad's skin may be activated in the presence of bacteria.
This is a complex defense mechanism of the toad, 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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