Using mirror-image peptides to enhance robustness and reproducibility in studying the amyloid β-protein

Alzheimer's disease, the most common form of dementia, is a devastating disease that affects over 44 million people worldwide. One etiological agent of Alzheimer's, the amyloid β-protein (Aβ), is an aggregation-prone, intrinsically disordered peptide that can form a wide variety of aggregates. The pathways by which Aβ aggregates in order to exert its toxicity, referred to as the Amyloid Cascade, remains largely elusive despite substantial deconvolution efforts. Preparing high-quality material that exhibits reproducible biophysical characteristics has proven challenging. Herein, we propose that mirror-image peptides can be used to rigorously control Aβ preparation quality.