The study investigates the inhibition of α-synuclein aggregation within liquid condensates, a process that may contribute to Parkinson's disease. The researchers found that claramine, an aminosterol, stabilizes α-synuclein condensates and inhibits aggregation both in vitro and in a Caenorhabditis elegans model of Parkinson's disease. Claramine shifts the phase boundary towards the condensed state, increasing the tendency of α-synuclein to phase separate. It also inhibits primary nucleation, reducing the rate of α-synuclein aggregation. In vivo, claramine administration in C. elegans reduced the number of α-synuclein inclusions, improved motility, and delayed the maturation of inclusions. These findings suggest a potential therapeutic route for preventing α-synuclein aggregation within condensates, which could be relevant for other neurodegenerative disorders.The study investigates the inhibition of α-synuclein aggregation within liquid condensates, a process that may contribute to Parkinson's disease. The researchers found that claramine, an aminosterol, stabilizes α-synuclein condensates and inhibits aggregation both in vitro and in a Caenorhabditis elegans model of Parkinson's disease. Claramine shifts the phase boundary towards the condensed state, increasing the tendency of α-synuclein to phase separate. It also inhibits primary nucleation, reducing the rate of α-synuclein aggregation. In vivo, claramine administration in C. elegans reduced the number of α-synuclein inclusions, improved motility, and delayed the maturation of inclusions. These findings suggest a potential therapeutic route for preventing α-synuclein aggregation within condensates, which could be relevant for other neurodegenerative disorders.