The aggregation of proteins in amyloid structures, a process described in mammals and fungus and bacteria, is implied in approximately 36 human diseases, including Alzheimer’s disease, Parkinson’s disease and type 2 diabetes. Most of the amyloid fibers are known for their ability to bind Congo Red (https://en.wikipedia.org/wiki/Congo_red), regarded as a specific marker of amyloid structures. This adds a great value to the compound Congo-Red, because it is one of the most used to detect the presence of amyloids and characterize the process of aggregation involved in amyloidogenic diseases. In a paper published online on February 19, 2020 in the journal Angewandte Chemistry International Edition, researchers at the University of Barcelona, and colleagues, identified the binding model of this dye. Specifically, the study focused on the interaction of Congo Red in amyloid structures formed by the HET-s (heterokaryon incompatibility protein s) prion particle (https://www.pnas.org/content/111/14/5201). The article is titled is titled ““On the binding of Congo Red to amyloid fibrils.” From a technological perspective, the results provide the molecular basis to explain the spectral changes in Congo Red when it joins amyloid fibers, which enables them to exploit this process in the study of aggregation of other proteins. Most important, is the fact that knowing this mechanism could enable researchers to identify potential strategies of inhibition of amyloid fibers involved in amyloid-origin diseases.
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