The conversion of a protein from its native state to stable fibrillar aggregates, such as amyloid fibrils, is a key process in protein chemistry, biology, medicine and biotechnology.
Our laboratory uses a multi-angle and multidisciplinary approach to study the fundamentals of protein aggregation and the mechanism by which the resulting aggregates cause cell dysfunction.
Amyloid fibrils are the “black hole” of the protein universe.
The amyloid structure is the most stable in the free energy landscape of a protein conformation, even more stable than the native state. And it has the ability to attract new protein molecules, thus resembling conceptually a black hole, which is a region of space from which nothing, including light, can escape.