6533b82dfe1ef96bd12914b5
RESEARCH PRODUCT
The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.
Valeria VetriVito Foderàsubject
Models MolecularAmyloidAmyloid Superstructures Protein aggregation spectroscopyProtein superstructureProtein ConformationBiophysicsNanotechnologyProtein aggregationProtein particulateBiochemistryProtein Aggregation PathologicalProtein AggregatesX-Ray DiffractionStructural BiologyElectrostaticsGeneticsHumansMolecular BiologyAmyloid likeAmyloid-like spheruliteChemistryCell BiologyConformational changeSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Microscopy Fluorescence MultiphotonModels ChemicalAggregate structureThermodynamicsExperimental methodsProtein aggregationdescription
AbstractDepending 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-09-01 | FEBS letters |