The molecular lifecycle of amyloid – Mechanism of assembly, mesoscopic organisation, polymorphism, suprastructures, and biological consequences

摘要: The formation of a diverse range amyloid structures from normally soluble proteins and peptides is hallmark devastating human disorders as well biological functions. current molecular understanding the lifecycle reveals four processes central to their growth propagation: primary nucleation, elongation, secondary nucleation division. However, these result in wide cross-β packing filament arrangements, including assemblies formed identical monomeric precursors with same amino acid sequences. Here, we review structural mechanistic self-assembly, discuss how mesoscopic, i.e. micrometre nanometre, organisation give rise suprastructural features that may be key link between polymorphic response they elicit. A greater mechanisms governing suprastructure will guide future strategies combat associated use control quaternary structure synthetic biology materials applications.