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 beta-protein (A beta), is an aggregation-prone, intrinsically disordered peptide that can form a wide variety of aggregates. The pathways by which A beta 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 A beta preparation quality.