Aggregation of an Amyloidogenic Peptide on Gold Surfaces

Solid surfaces have been shown to affect the aggregation and assembly of many biomolecular systems. One important example is the formation of protein fibrils, which can occur on a range of biological and synthetic surfaces. The rate of fibrillation depends on both the protein structure and the surface chemistry, with the different molecular and oligomer structures adopted by proteins on surfaces likely to be crucial. In this paper, the aggregation of the model amyloidogenic peptide, A beta(16-22), corresponding to a hydrophobic segment of the amyloid beta protein on a gold surface is studied using molecular dynamics simulation. Previous simulations of this peptide on gold surfaces have shown that it adopts conformations on surfaces that are quite different from those in bulk solution. These simulations show that this then leads to significant differences in the oligomer structures formed in solution and on gold surfaces. In particular, oligomers formed on the surface are low in beta-strands so are unlike the structures formed in bulk solution. When oligomers formed in solution adsorb onto gold surfaces they can then restructure themselves. This can then help explain the inhibition of A beta(16-22) fibrillation by gold surfaces and nanoparticles seen experimentally.

Automated summary

Solid surfaces have a significant impact on the aggregation and assembly of biomolecular systems, with protein fibrillation being an important example. The molecular and oligomer structures adopted by proteins on surfaces play a crucial role in the rate of fibrillation. Molecular dynamics simulation is used in this study to investigate the aggregation of a model amyloidogenic peptide on a gold surface. The simulations reveal that the peptide adopts different conformations on the surface compared to bulk solution, resulting in significant differences in the formed oligomer structures. The adsorption of oligomers on the surface can also lead to restructuring, offering an explanation for the inhibition of fibrillation observed experimentally.