A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers: A penetratin-derived peptide against α-synuclein oligomers.

ABSTRACT: Parkinson's Disease (PD) is a neurodegenerative movement disorder associated with the intracellular aggregation of α-synuclein (α-syn). Cytotoxicity is mainly associated with the oligomeric species (αSOs) formed at early stages in α-syn aggregation. Consequently, there is an intense focus on the discovery of novel inhibitors such as peptides to inhibit oligomer formation and toxicity. Here, using peptide arrays, we identified nine peptides with high specificity and affinity for αSOs. Of these, peptides p194, p235, and p249 diverted α-syn aggregation from fibrils to amorphous aggregates with reduced β-structures and increased random coil content. However, they did not reduce αSO's cytotoxicity and permeabilization of large anionic unilamellar vesicles (LUV). In parallel, we identified a non

SUBMITTER: Pirhaghi M 

PROVIDER: S-EPMC9791135 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature