Alpha-Synuclein-Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity.
Alpha-synuclein (αS) is an extensively studied protein due to its involvement in a group of neurodegenerative disorders, including Parkinson's disease, and its documented ability to undergo aberrant self-aggregation resulting in the formation of amyloid-like fibrils. In dilute solution, the protein is intrinsically disordered but can adopt multiple alternative conformations under given conditions, such as upon adsorption to nanoscale surfaces. The study of αS-nanoparticle interactions allows us to better understand the behavior of the protein and provides the basis for developing systems capable of mitigating the formation of toxic aggregates as well as for designing hybrid nanomaterials with novel functionalities for applications in various research areas. In this review, we summarize current progress on αS-nanoparticle interactions with an emphasis on the conformational plasticity of the biomolecule.
["D'Onofrio|Mariapina|M|0000-0002-8699-0847", 'Munari|Francesca|F|', 'Assfalg|Michael|M|0000-0001-9331-3169']
D000327:Adsorption D000682:Amyloid D006801:Humans D008968:Molecular Conformation D058726:Nanoconjugates D053758:Nanoparticles D066329:Protein Aggregates D051844:alpha-Synuclein
alpha-synuclein amyloid fibrils conformational flexibility nano-bio interface nanocomposite nanoparticles protein adsorption protein aggregation supramolecular assembly