ABSTRACT
The human muscle acylphosphatase (AcP) has been shown to form amyloid aggregates under mild denaturing conditions, i.e. in presence of 25% trifluoroethanol. This chapter explores the changes in the aggregates population after exposure to conditions that favour the native state. The size of the aggregates depends on the time of aggregation. The chapter suggests that the population of aggregates, at least in the case of AcP, is made of species with distinct sizes and thermodynamic properties. After the addition of 25% TFE, the protein partially unfolds; globular aggregates, proved to be bundles of protofilaments, develop progressively within 1-2 hours; they are able to form clusters of aggregates. The chapter provides a base for the design of appropriate approaches to the treatment of diseases associated with protein aggregation.
