News – Researchers at the Institute of Technology – Israel and the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, in collaboration with scientists in Israel and Spain, on features an amazing molecule of antimicrobial peptide obtained from the skin of an Australian toad. This discovery could stimulate the development of novel synthetic drugs to combat bacterial infections
An antibacterial peptide that turns on and off
The researchers unveiled the 3D molecular structure of an antibacterial peptide named uperin 3.5, which is secreted on the skin of Australian toads (Uperoleia mjobergii) as part of its immune system. They found that the peptide coalesces into a specific fibrous structure, which, through a vigorous structural modification mechanism, can change its shape in the presence of bacteria to protect the toad from disease. This provides specific evidence at the atomic level explaining the mode of administration of an antimicrobial peptide.
The antibacterial fibrils on the toad’s skin have a structure similar to amyloid fibrils, which are indicative of neurodegenerative diseases, such as Alzheimer’s and Parkinson’s. Although amyloid fibrils have been considered pathogenic for decades, it has recently been discovered that some amyloid fibrils can be beneficial to the organisms that make them, from humans to microbes. For example, certain bacteria secrete such fibrils to fight human immune cells.
The results show that the secretory antibacterial peptide on the toad’s skin combines in a “dormant” arrangement in the form of highly stable amyloid fibrils, which scientists explain. as a cross-β-concordance. These fibrils serve as a repository of invasive molecules that can be activated when bacteria are present. As soon as the peptide meets the bacterial membrane, it changes its molecular arrangement to a less tight α-form and changes to a lethal weapon. “This is a protective mechanism of the toad, stimulated by the invading bacteria themselves,” says Technion structural biologist, Professor Meytal Landau, lead author of this study. “This is a unique example of evolutionary design of movable supramolecular structures to control activity.”
Possible for future medical applications
Antimicrobial peptides are found in all realms of life, so they are thought to be commonly used as weapons in nature, sometimes effective in killing not only bacteria, but also cancer cells. . Moreover, the specific amyloid-like properties of the toadlet’s antibacterial peptide, found in this study, shed light on the possible physiological properties of amyloid fibrils associated with disorders. neurodegenerative and systemic.
The researchers hope that their discovery will lead to medical and technological applications, eg the development of synthetic antimicrobial peptides that would be activated only in the presence of bacteria. Synthetic peptides of this type could be a durable coating for medical devices or implants, or even in industrial equipment needed in sterile conditions.
The study is the result of a collaboration between scientists at EMBL Hamburg and Technion, and organizations in Israel and Spain. It is an example of the EMBL approach to life science research in the next Molecules to Ecosystems scientific program. EMBL incorporates interdisciplinary approaches to understand the basis of molecular life in the context of environmental change, and to provide translational capability to support advances in human and planetary health.
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