Acetylcholine hydrolytic activity of fibrillated -amyloid (1-40) peptide

Alzheimer's disease is characterized by the presence of senile plaques composed of beta-amyloid peptide (A beta) aggregates with toxic effects that are still not fully understood. Recently, it was discovered that A beta(1-42) fibrils possess catalytic activity on acetylcholine hydrolysis. Catalytic amyloids are an emerging and exciting field of research. In this study, we examined the catalytic activity of the fibrils formed by A beta(1-40), the most abundant A beta variant, on acetylcholine hydrolysis. Our findings reveal that A beta(1-40) fibrils exhibit moderate enzymatic activity, indicating that natural peptide aggregates could serve as biocatalysts and provide new insights into the potential role of A beta in neurological disorders.