{Reference Type}: Journal Article
{Title}: The antiviral drug Ribavirin effectively modulates the amyloid transformation of α-Synuclein protein.
{Author}: Singh P;Akhtar A;Admane N;Grover A;
{Journal}: Comput Biol Chem
{Volume}: 112
{Issue}: 0
{Year}: 2024 Jul 16
{Factor}: 3.737
{DOI}: 10.1016/j.compbiolchem.2024.108155
{Abstract}: α-Synuclein (α-syn) is an intrinsically disordered protein, linked genetically and neuropathologically to Parkinson's disease where this protein aggregates within the brain. Hence, identifying compounds capable of impeding α-syn aggregation puts forward a promising approach for the development of disease-modifying therapies. Herein, we investigated the efficacy of Ribavirin, an FDA-approved compound, in curtailing α-syn amyloid transformation, employing an array of bioinformatic tools and systematic analysis using biophysical techniques. Ribavirin shows a dose dependent anti-aggregation propensity where it effectively subdued the formation of mature fibrillar aggregates of α-syn, where even at the lowest concentration there was a 69 % reduction in the ThT maxima. Ribavirin averts the formation of mature fibrillar aggregates by interacting with the NAC domain of α-syn. Ribavirin redirects the amyloid transformation of α-syn by emanating aggregates of lower order with reduced cross β-sheet signature and revokes the formation of on-pathway amyloids. Collectively, our study puts forward the novel potency of Ribavirin as a promising molecule for therapeutic intervention in Parkinson's disease.