The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates
José D. Camino, Pablo Gracia, Serene W. Chen, Jesús Sot, Igor de la Arada, Víctor Sebastián, José L. R. Arrondo, Félix M. Goñi, Christopher M. Dobson, Nunilo Cremades
Abstract
α-synuclein aggregation where the protein can encounter a variety of hydration conditions in different cellular microenvironments, including the vicinity of lipid membranes or the interior of membraneless compartments, which could lead to the formation of remarkably different amyloid polymorphs by either heterogeneous or homogeneous nucleation.
Topics & Concepts
Antiparallel (mathematics)HomogeneousNucleationPreferenceBeta sheetChemical physicsChemistryMaterials scienceStatistical physicsProtein structurePhysicsMathematicsOrganic chemistryBiochemistryStatisticsMagnetic fieldQuantum mechanicsParkinson's Disease Mechanisms and Treatmentsbiodegradable polymer synthesis and propertiesPesticide and Herbicide Environmental Studies