A Cationic Zn-Phthalocyanine Turns Alzheimer's Amyloid β Aggregates into Non-Toxic Oligomers and Inhibits Neurotoxicity in Culture.

ABSTRACT: Amyloid β peptide (Aβ) aggregation and deposition are considered the main causes of Alzheimer's disease. In a previous study, we demonstrated that anionic Zn-phthalocyanine (ZnPc) can interact with the Aβ peptide and inhibit the fibril-formation process. However, due to the inability of anionic ZnPc to cross the intact blood-brain barrier, we decided to explore the interaction of cationic methylated Zn-phthalocyanine (cZnPc) with the peptide. Using a ThT fluorescence assay, we observed that cZnPc dose-dependently and time-dependently inhibited Aβ_1-42 fibril levels under in vitro fibril-formation conditions. Electron microscopy revealed that it caused Aβ_1-42 peptides to form small aggregates. Western blotting and dot immunoblot oligomer experiments demonstrated that cZ

SUBMITTER: Sheikh AM 

PROVIDER: S-EPMC11354870 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature