Amyloid fibers contribute to the development of neurodegenerative diseases such as Alzheimer's. Scientists are taking a closer look at these long chains of protein that line the neurons to better tackle them. Surprisingly, these fibrils have recently aroused significant interest in the nanotechnology sector. About one micron long and with a diameter is of the order of a few nanometers, they exhibit mechanical properties and shape factors (length/diameter) close to those of carbon nanotubes. They could therefore become a part of the new era of the nanoworld, which will use bioelectronics.

To be able to use these fibrils, the scientists need to precisely characterize them. Their structure has already been documented, but what about their mass? In collaboration with the Institut Lumière Matière in Lyon, researchers at our laboratory has answered that question. The researchers measured the mass of amyloid fibrils made of α-lactalbumin, a protein in whey, and Het-s, a filamentous fungus protein forming fibers. They used one of the two devices in the world capable of performing mass measurements on very large objects and whose molecular weight is around one gigadalton (GDa). The protocol used has made it possible to determine the average mass of a fiber as well as the mass distribution within a population of fibers. The next step will be to start over, but this time with fibers that are involved in neurodegenerative diseases.