title: The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.
abstract: Depending on external conditions, native proteins may change their structure and undergo different association routes leading to a large scale polymorphism of the aggregates. This feature has been widely observed but is not fully understood yet. This review focuses on morphologies, physico-chemical properties and mechanisms of formation of amyloid structures and protein superstructures. In particular, the main focus will be on protein particulates and amyloid-like spherulites, briefly summarizing possible experimental methods of analysis. Moreover, we will highlight the role of protein conformational changes and dominant forces in driving association together with their connection with the final aggregate structure. Eventually, we will discuss future perspectives in this field and we will comment what is, in our opinion, urgently needed.
authors.affiliation: Dipartimento di Fisica e Chimica, Università degli Studi di Palermo, Italy.
authors.forename: Valeria
authors.initials: V
authors.lastname: Vetri
authors.affiliation: Department of Pharmacy, Universitetsparken 2, University of Copenhagen, 2100 Copenhagen, Denmark. Electronic address: vito.fodera@sund.ku.dk.
authors.forename: Vito
authors.initials: V
authors.lastname: Foderà
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D006801:Humans; D036641:Microscopy, Fluorescence, Multiphoton; D008956:Models, Chemical; D008958:Models, Molecular; D066329:Protein Aggregates; D066263:Protein Aggregation, Pathological; D011487:Protein Conformation; D013816:Thermodynamics; D014961:X-Ray Diffraction
chemical_list: D000682:Amyloid; D066329:Protein Aggregates
keywords: Amyloid-like spherulite; Conformational change; Electrostatics; Protein aggregation; Protein particulate; Protein superstructure