Introduction
Amyloid-forming peptides and proteins underlie or are involved in devastating diseases including Alzheimer’s, Parkinson’s, Type 2 diabetes, and Creutzfeldt-Jakob (Mad Cow’s), and some cancers. Analyses of their structures, functions, and dysfunctions pose complicated problems that are difficult to solve. Amyloids are shape-shifters with a substantial amount of disorder. They adopt a plethora of secondary structures, conformations, and assemblies, these are often present simultaneously in dynamic equilibrium and depend upon numerous factors; e.g., peptide and salt concentrations, time, cofactors, post-translational modifications, and initial structure (seeds). α-Synuclein (α-Syn), a contributor to Parkinson’s Disease (PD), is a prime example (for recent review see Meade et al. [1]). Studies by Cremades et al. [2] illustrated the variance in oligomer sizes and how they alter as a function of time (Fig. 1). Similar results were obtained for the dissociation of fibrils into oligomers, demonstrating the dynamic nature of transitions among numerous semi-stable assemblies.