A study on amyloid fibrils, structures related to cell death triggered by neurodegenerative diseases such as Alzheimer's or Parkinson's, describes, for the first time, the dynamics of these fibrils and the possibility to establish the parameters that characterize this movement. This discovery, made by researchers at the Institute of Biomedical Research of the Parc Científic de Barcelona (IRB-PCB) and by the University of Cambridge, will allow scientists to initiate new lines of research to find new drugs that can be used to treat these diseases. The results from this study have been published in the edition of the scientific journal Nature released on 28 July.

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The research has been performed in collaboration between the group “Design, Synthesis and Structure of Peptides and Proteins” at the IRB-PCB, directed by Ernest Giralt, researcher and professor with the Dept. of Organic Chemistry at the Universitat de Barcelona (University of Barcelona, UB), and the teams led by professors Carol V. Robinson and Christopher M. Dobson at the Dept. Of Chemistry at the University of Cambridge. The work has focused on amyloid fibrils through the study of the aggregation of certain proteins, which stack on top of one another.

Until now, it was not known whether amyloid fibrils were static or dynamic structures. “In this study we have observed that the amyloid aggregates are dynamic, i.e. protein molecules that comprise the fibrils are “recycling”. We have been able to demonstrate how several molecules that form part of the fibril disassociate from this structure in certain instances, to later reincorporate into the fibril. This observation paves the way for the design of drugs able to adhere to protein molecules that disassociate from the fibril in such a way as to prevent the molecules from reincorporating, thereby causing the dissolution of these structures. This capacity could be used in the treatment of diseases in which amyloid proteins are involved”, commented Ernest Giralt.

In the case of Alzheimer’s disease, amyloid fibrils form plaques at the connection points between neurons, thereby preventing the transmission of neuronal information and disconnecting areas of the brain that normally work in unison. These results open up a new avenue of study into therapeutic strategies for the prevention and treatment of the disease by acting on fibrils and on the formation of plaques.

The new study has arisen from research performed by the investigator with the IRB-PCB Natàlia Carulla, who, during the last four years, has been working in the laboratories of the two institutions. The researchers involved in this study have examined a model proteins using techniques such as mass spectrometry and nuclear magnetic resonance. The latter technique has also involved the collaboration of Miguel Feliz and Margarida Gairí, members of the Nuclear Magnetic Resonance Unit of the Scientific and Technical Services of the UB, also located at the Parc Científic de Barcelona.