Cornejo, AlbertoCaballero, JulioSimirgiotis, MarioTorres, VanessaSánchez, LuisaDíaz, NicolásGuimaraes, MarcelaHernández, MarcosAreche, CarlosAlfaro, SergioCaballero, LeonardoMelo, Francisco2022-06-132022-06-132021Journal of Enzyme Inhibition and Medicinal Chemistry Volume 36 Issue 1 Pages 154 - 16220211475-6366https://repositorio.unab.cl/xmlui/handle/ria/22778Indexación ScopusParkinson's disease (PD) is a neurodegenerative disorder that affects adult people whose treatment is palliative. Thus, we decided to test three dammarane triterpenes 1, 1a, 1b, and we determined that 1 and 1a inhibit β-aggregation through thioflavine T rather than 1b. Since compound 1 was most active, we determined the interaction between α-synuclein and 1 at 50 µM (Kd) through microscale thermophoresis. Also, we observed differences in height and diameter of aggregates, and α-synuclein remains unfolded in the presence of 1. Also, aggregates treated with 1 do not provoke neurites' retraction in N2a cells previously induced by retinoic acid. Finally, we studied the potential sites of interaction between 1 with α-synuclein fibrils using molecular modelling. Docking experiments suggest that 1 preferably interact with the site 2 of α-synuclein through hydrogen bonds with residues Y39 and T44.endrug targetnatural compounds modifiersoligomersParkinson’s diseaseArtículoAttribution 4.0 International (CC BY 4.0)10.1080/14756366.2020.1851216