Self-assembly of amyloid-like peptides at interfaces investigated by atomic force microscopy

In the past few years, numerous researches have focused on the self-assembly of amyloid peptides and proteins. Especially, the self-assembly of peptides and proteins at interfaces has attracted much attention, on account of the potential applications as well as understanding mechanism of some neurodegenerative diseases. In this review, we centered topic on recent progress of the self-assembly of amyloid-like peptides at interfaces, which was mainly carried out in our group by employing atomic force microscopy (AFM). In the first part of the review, we introduced how the amyloid peptides assembled at the solid substrate/water interface. And nanoscale control of the assembly of the peptides by AFM has also been introduced. In the second part of this review, we focused on how the amyloid-like peptides assembled at air/solid interface, in which diffusion and self-assembly of peptides occurred with the help of a water nanofilm confined from ambient environment onto the solid surface. These results indicate that interfaces play an important role in peptide assembly, and also prove that AFM is one of the powerful instruments in studying peptide self-assembly.