Membrane−Protein Interactions Are Key to Understanding Amyloid Formation

Spurred by the appreciation that protein aggregation, leadingto amyloid fibril formation, is linked to a growing list of diseases, there has been intense effort to understand the factors that trigger association between peptides. This vastly complex field has attracted a variety of approaches ranging from mutational studies at the genetic level to characterization of events at the molecular level of specific proteins. It is unclear if biophysical approaches used to study protein folding in quantitative terms will have a major impact on leading to a cure or management of any amyloid disease, including Alzheimer’s Disease (AD). Nevertheless, it is clear that rigorous biophysical methods are needed to gain a deeper understanding of the routes to amyloid formation. After nearly 15 years of in vitro experimentation and simulations, certain general principles that govern oligomer (suspected to be the cause of toxicity) and amyloid formation have emerged. A few of th