Abstract
Amyloid fibrils generally have a cross –β structure, in which β– strands are stacked in the axial direction of the fibril. Probably because of this periodic structure, the formation of amyloid fibrils is similar to that of crystals, and the nucleation process is observed in early stages, acting as a rate–determining step. This article outlines the basic properties of amyloid fibril nucleation in the light of the nucleation theory proposed for crystallization. I also discuss how amyloid nucleation is affected at a lipid membrane interface in order to understand the mechanism of amyloid fibril formation in biological systems.
