A peptide probe for detection of various beta-amyloid oligomers

摘要: Aggregation of β-amyloid (Aβ) is implicated in the pathology Alzheimer's disease (AD). A considerable amount data has identified soluble Aβ oligomers as potentially significant toxic agents. Rapid, specific and quantitative detection preferred for accurate profiling structurally unstable well implementation high-throughput assays pharmaceutical applications. PG46 an engineered variant, constructed by integrating self-recognition sequences with conformation-sensitive biarsenical fluorescent dye, FlAsH. was found to be effective peptide probe, which detected specifically quantitatively within one hour. However, highly aggregation-prone displayed a limited repertoire detectable oligomers. Here, we report creation novel molecular PG44, C-terminal truncation PG46. PG44 exhibited reduced self-aggregation propensity different conformation when compared PG46, generated FlAsH fluorescence signals result binding various oligomers, including those not readily We also show that sensitivity certain may increased lowering concentration thus decreasing extent PG44. Our results suggest can serve important probe broadened oligomeric aggregates. believe using our would contribute toward better understanding basis oligomerization development oligomer-based early diagnostics therapeutic drugs targeting