Soluble cytotoxic oligomers produced during the fibrillation of both α-synuclein (αS) and amyloid-β protein (Aβ) are key pathogenic factors in Parkinson's disease (PD) and Alzheimer's disease (AD). Reducing toxic oligomers by regulating the aggregation process of αS and Aβ is an important strategy for the treatment of PD and AD. Herein, tetrahydrofolic acid (THF) is found to accelerate amyloid fibrillization, decreases cytotoxic oligomers and suppresses their toxicity. Thioflavin T and atomic force microscopy assays results showed that THF was able to accelerate the formation of dense fibrils from αS and Aβ in a dose-dependent manner. Strikingly, this was accompanied by a reduction in the abundance of toxic oligomers, and these results were confirmed by DB. Meanwhile, MTT and FDA/PI assays demonstrated that THF-induced accelerated fibril formation was accompanied by a reduction in αS- and Aβ-induced cytotoxicity. In addition, the lifespan of genetically modified αS and Aβ expressing C. elegans was extended by feeding THF, although plaque deposits of αS and Aβ increased. These findings suggest that THF enhances the conversion of αS and Aβ oligomers into less toxic fibrils and is a potential therapeutic agent for PD and AD.