The presence of surfaces influences
the kinetics of amyloid-β
(Aβ) peptide fibrillation. Although it has been generally recognized
that the fibrillation process can be assisted or accelerated by surface
chemistry, the impact of surface topography, i.e., roughness, on peptide
fibrillation is relatively little understood. Here we study the role
of surface roughness on surface-mediated fibrillation using polymer
coatings of varying roughness as well as polymer microparticles. Using
single-molecule tracking, atomic force microscopy, and the thioflavin
T fluorescence technique, we show that a rough surface decelerates
the two-dimensional (2D) diffusion of peptides and retards the surface-mediated
fibrillation. A higher degree of roughness that presents an obstacle
to peptide diffusion is found to inhibit the fibrillation process
