Gold nanocolloid-protein interactions and their impact on β-sheet amyloid fibril formation

The influence of the presence of small molecules and nanoparticles on the mechanism of amyloid fibril formation has attracted attention because amyloid protein fibrils are associated with degenerative diseases. Here, we studied the interaction between gold nanoparticles (AuNPs) and a model protein (lysozyme). Both the formation of amyloid fibrils in the presence of gold nanoparticles, as well as the interaction between lysozyme and the amyloid fibrils with AuNPs, were investigated to gain an understanding of the distinct behaviour of lysozyme in its fibrillar and globular form. It was observed that the presence of AuNPs delayed the unfolding of α-helixes present in the globular lysozyme and the formation of the amyloid fibrils. However, the addition of AuNPs was also associated with a larger amount of β-sheet structures in the system once equilibrium was reached. Furthermore, the results showed that the driving force of the interaction between AuNPs and lysozyme in its fibrillar and globular forms was significantly different, and that the interaction of AuNPs with the preformed lysozyme amyloid fibrils led to a structural change in the protein. Formation of amyloid protein fibrils is associated with degenerative diseases. Here, the interaction mechanism between globular and fibrillar proteins with AuNPs were investigated in order to potentially control and reverse the fibrillation process.