Self-organization of short peptide fragments: From amyloid fibrils to nanoscale supramolecular assemblies

Numerous supramolecular protein assemblies had been demonstrated to have either physiological or pathological activities. The most significant case of disease-associated self-organized structures is that of amyloid fibrils. The formation of these fibrils is the hallmark of major human disorders, including Alzheimer's disease and type II diabetes. In this review we illustrate the molecular properties of the amyloid fibrils as supramolecular assemblies in the nanometric scale. We present recent advances in the elucidation of the molecular recognition and self-assembly processes that lead to the formation of these toxic structures, and we describe how the mechanistic study of amyloid formation process has led to unexpected discoveries of peptide-based nanostructures.