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The presence of oligomeric aggregates, which is often observed during theprocess of amyloid formation, has recently attracted much attention since ithas been associated with neurodegenerative conditions such as Alzheimer's andParkinson's diseases. We provide a description of a sequence-indepedentmechanism by which polypeptide chains aggregate by forming metastableoligomeric intermediate states prior to converting into fibrillar structures.Our results illustrate how the formation of ordered arrays of hydrogen bondsdrives the formation of beta-sheets within the disordered oligomeric aggregatesthat form early under the effect of hydrophobic forces. Initially individualbeta-sheets form with random orientations, which subsequently tend to aligninto protofilaments as their lengths increases. Our results suggest thatamyloid aggregation represents an example of the Ostwald step rule of firstorder phase transitions by showing that ordered cross-beta structures emergepreferentially from disordered compact dynamical intermediate assemblies.

Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric aggregates